3exh - Revision history

OCA at 00:26, 28 December 2023

OCA — Thu, 28 Dec 2023 00:26:03 GMT

←Older revision		Revision as of 00:26, 28 December 2023
Line 3:		Line 3:
	<StructureSection load='3exh' size='340' side='right'caption='[[3exh]], [[Resolution\|resolution]] 2.44Å' scene=''>		<StructureSection load='3exh' size='340' side='right'caption='[[3exh]], [[Resolution\|resolution]] 2.44Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3exh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EXH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3exh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EXH FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>~~, ~~<scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.444Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~SEP~~:~~PHOSPHOSERINE~~'>~~SEP~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td><~~td class~~=~~"sblockDat"><div style~~=~~'overflow~~: ~~auto; max-height: 3em;~~'>~~[[3exe\|3exe]], [[3exf\|3exf]], [[3exg\|3exg]], [[3exi\|3exi]]~~</~~div~~><~~/td></tr>~~	+
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></~~td><td class="sblockDat"~~>~~PDHA1~~, PHE1A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PDHB, PHE1B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])<~~/td></tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>[https://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3exh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exh OCA], [https://pdbe.org/3exh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3exh RCSB], [https://www.ebi.ac.uk/pdbsum/3exh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3exh ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3exh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exh OCA], [https://pdbe.org/3exh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3exh RCSB], [https://www.ebi.ac.uk/pdbsum/3exh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3exh ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] Defects in PDHA1 are a cause of pyruvate dehydrogenase E1-alpha deficiency (PDHAD) [MIM:[https://omim.org/entry/312170 312170]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:1338114</ref> <ref>PMID:1909401</ref> <ref>PMID:1551669</ref> <ref>PMID:1293379</ref> <ref>PMID:8504306</ref> <ref>PMID:8032855</ref> <ref>PMID:7545958</ref> <ref>PMID:7967473</ref> <ref>PMID:7887409</ref> <ref>PMID:7573035</ref> <ref>PMID:7757088</ref> <ref>PMID:8664900</ref> <ref>PMID:8844217</ref> <ref>PMID:9671272</ref> Defects in PDHA1 are the cause of X-linked Leigh syndrome (X-LS) [MIM:[https://omim.org/entry/308930 308930]]. X-LS is an early-onset progressive neurodegenerative disorder with a characteristic neuropathology consisting of focal, bilateral lesions in one or more areas of the central nervous system, including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord. The lesions are areas of demyelination, gliosis, necrosis, spongiosis, or capillary proliferation. Clinical symptoms depend on which areas of the central nervous system are involved. The most common underlying cause is a defect in oxidative phosphorylation. LS may be a feature of a deficiency of any of the mitochondrial respiratory chain complexes.<ref>PMID:1909401</ref> <ref>PMID:7887409</ref> <ref>PMID:8498846</ref> <ref>PMID:8199595</ref> <ref>PMID:9266390</ref> [[https://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] Defects in PDHB are the cause of pyruvate dehydrogenase E1-beta deficiency (PDHBD) [MIM:[https://omim.org/entry/614111 614111]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:15138885</ref>	+	[https://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN] Defects in PDHA1 are a cause of pyruvate dehydrogenase E1-alpha deficiency (PDHAD) [MIM:[https://omim.org/entry/312170 312170]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:1338114</ref> <ref>PMID:1909401</ref> <ref>PMID:1551669</ref> <ref>PMID:1293379</ref> <ref>PMID:8504306</ref> <ref>PMID:8032855</ref> <ref>PMID:7545958</ref> <ref>PMID:7967473</ref> <ref>PMID:7887409</ref> <ref>PMID:7573035</ref> <ref>PMID:7757088</ref> <ref>PMID:8664900</ref> <ref>PMID:8844217</ref> <ref>PMID:9671272</ref> Defects in PDHA1 are the cause of X-linked Leigh syndrome (X-LS) [MIM:[https://omim.org/entry/308930 308930]. X-LS is an early-onset progressive neurodegenerative disorder with a characteristic neuropathology consisting of focal, bilateral lesions in one or more areas of the central nervous system, including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord. The lesions are areas of demyelination, gliosis, necrosis, spongiosis, or capillary proliferation. Clinical symptoms depend on which areas of the central nervous system are involved. The most common underlying cause is a defect in oxidative phosphorylation. LS may be a feature of a deficiency of any of the mitochondrial respiratory chain complexes.<ref>PMID:1909401</ref> <ref>PMID:7887409</ref> <ref>PMID:8498846</ref> <ref>PMID:8199595</ref> <ref>PMID:9266390</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:7782287</ref> <ref>PMID:19081061</ref> [[https://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:17474719</ref> <ref>PMID:19081061</ref>	+	[https://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:7782287</ref> <ref>PMID:19081061</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chuang~~, D T~~]]	+	[[Category: Chuang DT]]
-	[[Category: Chuang~~, J L~~]]	+	[[Category: Chuang JL]]
-	[[Category: Kato, M]]	+	[[Category: Kato M]]
-	[[Category: Li, J]]	+	[[Category: Li J]]
-	[[Category: Machius, M]]	+	[[Category: Machius M]]
-	[[Category: Tso, S C]]	+	[[Category: Tso S-C]]
-	[[Category: Wynn~~, R M]]~~	+	[[Category: Wynn RM]]
-	~~[[Category: Alternative splicing]]~~	+
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Glycolysis]]~~	+
-	~~[[Category: Heterotetramer]]~~	+
-	~~[[Category: Leigh syndrome]]~~	+
-	~~[[Category: Mitochondrion]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: Pyruvate]]~~	+
-	~~[[Category: Thiamine diphosphate-dependent enzyme]]~~	+
-	~~[[Category: Thiamine pyrophosphate]]~~	+
-	~~[[Category: Transit peptide~~]]	+

OCA at 19:47, 20 October 2021

OCA — Wed, 20 Oct 2021 19:47:47 GMT

←Older revision		Revision as of 19:47, 20 October 2021
Line 1:		Line 1:

	==Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex==		==Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex==
-	<StructureSection load='3exh' size='340' side='right' caption='[[3exh]], [[Resolution\|resolution]] 2.44Å' scene=''>	+	<StructureSection load='3exh' size='340' side='right'caption='[[3exh]], [[Resolution\|resolution]] 2.44Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3exh]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3EXH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3exh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EXH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3exe\|3exe]], [[3exf\|3exf]], [[3exg\|3exg]], [[3exi\|3exi]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3exe\|3exe]], [[3exf\|3exf]], [[3exg\|3exg]], [[3exi\|3exi]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PDHA1, PHE1A ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PDHB, PHE1B ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PDHA1, PHE1A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PDHB, PHE1B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3exh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exh OCA], [~~http~~://pdbe.org/3exh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3exh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3exh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3exh ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3exh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exh OCA], [https://pdbe.org/3exh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3exh RCSB], [https://www.ebi.ac.uk/pdbsum/3exh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3exh ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] Defects in PDHA1 are a cause of pyruvate dehydrogenase E1-alpha deficiency (PDHAD) [MIM:[~~http~~://omim.org/entry/312170 312170]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:1338114</ref> <ref>PMID:1909401</ref> <ref>PMID:1551669</ref> <ref>PMID:1293379</ref> <ref>PMID:8504306</ref> <ref>PMID:8032855</ref> <ref>PMID:7545958</ref> <ref>PMID:7967473</ref> <ref>PMID:7887409</ref> <ref>PMID:7573035</ref> <ref>PMID:7757088</ref> <ref>PMID:8664900</ref> <ref>PMID:8844217</ref> <ref>PMID:9671272</ref> Defects in PDHA1 are the cause of X-linked Leigh syndrome (X-LS) [MIM:[~~http~~://omim.org/entry/308930 308930]]. X-LS is an early-onset progressive neurodegenerative disorder with a characteristic neuropathology consisting of focal, bilateral lesions in one or more areas of the central nervous system, including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord. The lesions are areas of demyelination, gliosis, necrosis, spongiosis, or capillary proliferation. Clinical symptoms depend on which areas of the central nervous system are involved. The most common underlying cause is a defect in oxidative phosphorylation. LS may be a feature of a deficiency of any of the mitochondrial respiratory chain complexes.<ref>PMID:1909401</ref> <ref>PMID:7887409</ref> <ref>PMID:8498846</ref> <ref>PMID:8199595</ref> <ref>PMID:9266390</ref> [[~~http~~://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] Defects in PDHB are the cause of pyruvate dehydrogenase E1-beta deficiency (PDHBD) [MIM:[~~http~~://omim.org/entry/614111 614111]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:15138885</ref>	+	[[https://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] Defects in PDHA1 are a cause of pyruvate dehydrogenase E1-alpha deficiency (PDHAD) [MIM:[https://omim.org/entry/312170 312170]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:1338114</ref> <ref>PMID:1909401</ref> <ref>PMID:1551669</ref> <ref>PMID:1293379</ref> <ref>PMID:8504306</ref> <ref>PMID:8032855</ref> <ref>PMID:7545958</ref> <ref>PMID:7967473</ref> <ref>PMID:7887409</ref> <ref>PMID:7573035</ref> <ref>PMID:7757088</ref> <ref>PMID:8664900</ref> <ref>PMID:8844217</ref> <ref>PMID:9671272</ref> Defects in PDHA1 are the cause of X-linked Leigh syndrome (X-LS) [MIM:[https://omim.org/entry/308930 308930]]. X-LS is an early-onset progressive neurodegenerative disorder with a characteristic neuropathology consisting of focal, bilateral lesions in one or more areas of the central nervous system, including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord. The lesions are areas of demyelination, gliosis, necrosis, spongiosis, or capillary proliferation. Clinical symptoms depend on which areas of the central nervous system are involved. The most common underlying cause is a defect in oxidative phosphorylation. LS may be a feature of a deficiency of any of the mitochondrial respiratory chain complexes.<ref>PMID:1909401</ref> <ref>PMID:7887409</ref> <ref>PMID:8498846</ref> <ref>PMID:8199595</ref> <ref>PMID:9266390</ref> [[https://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] Defects in PDHB are the cause of pyruvate dehydrogenase E1-beta deficiency (PDHBD) [MIM:[https://omim.org/entry/614111 614111]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:15138885</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:7782287</ref> <ref>PMID:19081061</ref> [[~~http~~://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:17474719</ref> <ref>PMID:19081061</ref>	+	[[https://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:7782287</ref> <ref>PMID:19081061</ref> [[https://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:17474719</ref> <ref>PMID:19081061</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ex/3exh_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ex/3exh_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 34:		Line 34:
	</div>		</div>
	<div class="pdbe-citations 3exh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3exh" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Pyruvate dehydrogenase 3D structures\|Pyruvate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 42:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Chuang, D T]]		[[Category: Chuang, D T]]
	[[Category: Chuang, J L]]		[[Category: Chuang, J L]]

OCA at 09:22, 25 October 2017

OCA — Wed, 25 Oct 2017 09:22:32 GMT

←Older revision		Revision as of 09:22, 25 October 2017
Line 1:		Line 1:
		+
	==Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex==		==Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex==
	<StructureSection load='3exh' size='340' side='right' caption='[[3exh]], [[Resolution\|resolution]] 2.44Å' scene=''>		<StructureSection load='3exh' size='340' side='right' caption='[[3exh]], [[Resolution\|resolution]] 2.44Å' scene=''>
Line 8:		Line 9:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PDHA1, PHE1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PDHB, PHE1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PDHA1, PHE1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PDHB, PHE1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3exh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exh OCA], [http://pdbe.org/3exh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3exh RCSB], [http://www.ebi.ac.uk/pdbsum/3exh PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3exh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exh OCA], [http://pdbe.org/3exh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3exh RCSB], [http://www.ebi.ac.uk/pdbsum/3exh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3exh ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 33:		Line 34:
	</div>		</div>
	<div class="pdbe-citations 3exh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3exh" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Pyruvate dehydrogenase\|Pyruvate dehydrogenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:10, 8 February 2016

OCA — Mon, 08 Feb 2016 12:10:46 GMT

←Older revision		Revision as of 12:10, 8 February 2016
Line 2:		Line 2:
	<StructureSection load='3exh' size='340' side='right' caption='[[3exh]], [[Resolution\|resolution]] 2.44Å' scene=''>		<StructureSection load='3exh' size='340' side='right' caption='[[3exh]], [[Resolution\|resolution]] 2.44Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3exh]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EXH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3exh]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EXH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3exe\|3exe]], [[3exf\|3exf]], [[3exg\|3exg]], [[3exi\|3exi]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3exe\|3exe]], [[3exf\|3exf]], [[3exg\|3exg]], [[3exi\|3exi]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PDHA1, PHE1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), PDHB, PHE1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PDHA1, PHE1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PDHB, PHE1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3exh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3exh RCSB], [http://www.ebi.ac.uk/pdbsum/3exh PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3exh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exh OCA], [http://pdbe.org/3exh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3exh RCSB], [http://www.ebi.ac.uk/pdbsum/3exh PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 22:		Line 22:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3exh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 32:		Line 32:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3exh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 39:		Line 40:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Chuang, D T]]		[[Category: Chuang, D T]]
	[[Category: Chuang, J L]]		[[Category: Chuang, J L]]

OCA at 14:19, 18 December 2014

OCA — Thu, 18 Dec 2014 14:19:52 GMT

←Older revision		Revision as of 14:19, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3exh~~\| ~~PDB~~=3exh \| ~~SCENE~~= }}	+	==Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex==
-	===~~Crystal~~ structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex~~===~~	+	<StructureSection load='3exh' size='340' side='right' caption='[[3exh]], [[Resolution\|resolution]] 2.44Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19081061}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3exh]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EXH FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3exe\|3exe]], [[3exf\|3exf]], [[3exg\|3exg]], [[3exi\|3exi]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PDHA1, PHE1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), PDHB, PHE1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3exh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3exh RCSB], [http://www.ebi.ac.uk/pdbsum/3exh PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] Defects in PDHA1 are a cause of pyruvate dehydrogenase E1-alpha deficiency (PDHAD) [MIM:[http://omim.org/entry/312170 312170]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:1338114</ref> <ref>PMID:1909401</ref> <ref>PMID:1551669</ref> <ref>PMID:1293379</ref> <ref>PMID:8504306</ref> <ref>PMID:8032855</ref> <ref>PMID:7545958</ref> <ref>PMID:7967473</ref> <ref>PMID:7887409</ref> <ref>PMID:7573035</ref> <ref>PMID:7757088</ref> <ref>PMID:8664900</ref> <ref>PMID:8844217</ref> <ref>PMID:9671272</ref> Defects in PDHA1 are the cause of X-linked Leigh syndrome (X-LS) [MIM:[http://omim.org/entry/308930 308930]]. X-LS is an early-onset progressive neurodegenerative disorder with a characteristic neuropathology consisting of focal, bilateral lesions in one or more areas of the central nervous system, including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord. The lesions are areas of demyelination, gliosis, necrosis, spongiosis, or capillary proliferation. Clinical symptoms depend on which areas of the central nervous system are involved. The most common underlying cause is a defect in oxidative phosphorylation. LS may be a feature of a deficiency of any of the mitochondrial respiratory chain complexes.<ref>PMID:1909401</ref> <ref>PMID:7887409</ref> <ref>PMID:8498846</ref> <ref>PMID:8199595</ref> <ref>PMID:9266390</ref> [[http://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] Defects in PDHB are the cause of pyruvate dehydrogenase E1-beta deficiency (PDHBD) [MIM:[http://omim.org/entry/614111 614111]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:15138885</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:7782287</ref> <ref>PMID:19081061</ref> [[http://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:17474719</ref> <ref>PMID:19081061</ref>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ex/3exh_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	We report the crystal structures of the phosporylated pyruvate dehydrogenase (E1p) component of the human pyruvate dehydrogenase complex (PDC). The complete phosphorylation at Ser264-alpha (site 1) of a variant E1p protein was achieved using robust pyruvate dehydrogenase kinase 4 free of the PDC core. We show that unlike its unmodified counterpart, the presence of a phosphoryl group at Ser264-alpha prevents the cofactor thiamine diphosphate-induced ordering of the two loops carrying the three phosphorylation sites. The disordering of these phosphorylation loops is caused by a previously unrecognized steric clash between the phosphoryl group at site 1 and a nearby Ser266-alpha, which nullifies a hydrogen-bonding network essential for maintaining the loop conformations. The disordered phosphorylation loops impede the binding of lipoyl domains of the PDC core to E1p, negating the reductive acetylation step. This results in the disruption of the substrate channeling in the PDC, leading to the inactivation of this catalytic machine.

-	~~==Disease==~~	+	Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops.,Kato M, Wynn RM, Chuang JL, Tso SC, Machius M, Li J, Chuang DT Structure. 2008 Dec 10;16(12):1849-59. PMID:19081061<ref>PMID:19081061</ref>
-	~~[[http://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] Defects in PDHA1 are a cause~~ of pyruvate dehydrogenase ~~E1-alpha deficiency (PDHAD) [MIM~~:[http://omim.org/entry/312170 312170]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:1338114</ref><ref>PMID:1909401</ref><ref>PMID:1551669</ref><ref>PMID:1293379</ref><ref>PMID:8504306</ref><ref>PMID:8032855</ref><ref>PMID:7545958</ref><ref>PMID:7967473</ref><ref>PMID:7887409</ref><ref>PMID:7573035</ref><ref>PMID:7757088</ref><ref>PMID:8664900</ref><ref>PMID:8844217</ref><ref>PMID:9671272</ref> Defects in PDHA1 are the cause of ~~X-linked Leigh syndrome (X-LS) [MIM:[http://omim~~.~~org/entry/308930 308930]]. X-LS is an early-onset progressive neurodegenerative disorder with a characteristic neuropathology consisting of focal~~, ~~bilateral lesions in one or more areas of the central nervous system~~, ~~including the brainstem~~, ~~thalamus~~, ~~basal ganglia~~, ~~cerebellum~~, ~~and spinal cord. The lesions are areas of demyelination~~, ~~gliosis, necrosis, spongiosis, or capillary proliferation~~. Clinical symptoms depend on which areas of the central nervous system are involved. The most common underlying cause is a defect in oxidative phosphorylation. LS may be a feature of a deficiency of any of the mitochondrial respiratory chain complexes.<ref>PMID:1909401</ref><ref>PMID:7887409</ref><ref>PMID:8498846</ref><ref>PMID:8199595</ref><ref>PMID:9266390</ref> [[http://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] Defects in PDHB are the cause of pyruvate dehydrogenase E1-beta deficiency (~~PDHBD~~) ~~[MIM~~:~~[http~~://omim.org/entry/614111 614111]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:~~15138885~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion~~ of ~~pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to~~ the ~~tricarboxylic cycle~~.~~<ref>PMID:7782287</ref><ref>PMID:19081061</ref> [[http://www~~.~~uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion~~ of ~~pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle~~.<~~ref~~>~~PMID:17474719~~</~~ref~~>~~<ref>PMID:19081061</ref>~~	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[3exh]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA].	+

	==See Also==		==See Also==
	*[[Pyruvate dehydrogenase\|Pyruvate dehydrogenase]]		*[[Pyruvate dehydrogenase\|Pyruvate dehydrogenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019081061</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Chuang, D T.]]	+	[[Category: Chuang, D T]]
-	[[Category: Chuang, J L.]]	+	[[Category: Chuang, J L]]
-	[[Category: Kato, M.]]	+	[[Category: Kato, M]]
-	[[Category: Li, J.]]	+	[[Category: Li, J]]
-	[[Category: Machius, M.]]	+	[[Category: Machius, M]]
-	[[Category: Tso, S C.]]	+	[[Category: Tso, S C]]
-	[[Category: Wynn, R M.]]	+	[[Category: Wynn, R M]]
	[[Category: Alternative splicing]]		[[Category: Alternative splicing]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]

OCA at 11:46, 24 March 2013

OCA — Sun, 24 Mar 2013 11:46:30 GMT

←Older revision		Revision as of 11:46, 24 March 2013
Line 1:		Line 1:
-	[[Image:3exh.png\|left\|200px]]
-
	{{STRUCTURE_3exh\| PDB=3exh \| SCENE= }}		{{STRUCTURE_3exh\| PDB=3exh \| SCENE= }}
-
	===Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex===		===Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex===
		+	{{ABSTRACT_PUBMED_19081061}}

-	~~{{ABSTRACT_PUBMED_19081061}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] Defects in PDHA1 are a cause of pyruvate dehydrogenase E1-alpha deficiency (PDHAD) [MIM:[http://omim.org/entry/312170 312170]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:1338114</ref><ref>PMID:1909401</ref><ref>PMID:1551669</ref><ref>PMID:1293379</ref><ref>PMID:8504306</ref><ref>PMID:8032855</ref><ref>PMID:7545958</ref><ref>PMID:7967473</ref><ref>PMID:7887409</ref><ref>PMID:7573035</ref><ref>PMID:7757088</ref><ref>PMID:8664900</ref><ref>PMID:8844217</ref><ref>PMID:9671272</ref> Defects in PDHA1 are the cause of X-linked Leigh syndrome (X-LS) [MIM:[http://omim.org/entry/308930 308930]]. X-LS is an early-onset progressive neurodegenerative disorder with a characteristic neuropathology consisting of focal, bilateral lesions in one or more areas of the central nervous system, including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord. The lesions are areas of demyelination, gliosis, necrosis, spongiosis, or capillary proliferation. Clinical symptoms depend on which areas of the central nervous system are involved. The most common underlying cause is a defect in oxidative phosphorylation. LS may be a feature of a deficiency of any of the mitochondrial respiratory chain complexes.<ref>PMID:1909401</ref><ref>PMID:7887409</ref><ref>PMID:8498846</ref><ref>PMID:8199595</ref><ref>PMID:9266390</ref> [[http://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] Defects in PDHB are the cause of pyruvate dehydrogenase E1-beta deficiency (PDHBD) [MIM:[http://omim.org/entry/614111 614111]]. An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.<ref>PMID:15138885</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/ODPA_HUMAN ODPA_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:7782287</ref><ref>PMID:19081061</ref> [[http://www.uniprot.org/uniprot/ODPB_HUMAN ODPB_HUMAN]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.<ref>PMID:17474719</ref><ref>PMID:19081061</ref>

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019081061</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019081061</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chuang, D T.]]		[[Category: Chuang, D T.]]

OCA at 10:05, 20 October 2012

OCA — Sat, 20 Oct 2012 10:05:22 GMT

←Older revision		Revision as of 10:05, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[3exh]] is a 8 chain structure ~~of [[Pyruvate dehydrogenase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA].	+	[[3exh]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA].

	==See Also==		==See Also==

OCA: Protected "3exh" [edit=sysop:move=sysop]

OCA — Thu, 26 Jul 2012 00:56:48 GMT

Protected "3exh" [edit=sysop:move=sysop]

←Older revision

Revision as of 00:56, 26 July 2012

OCA at 00:56, 26 July 2012

OCA — Thu, 26 Jul 2012 00:56:46 GMT

←Older revision		Revision as of 00:56, 26 July 2012
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-	{{Seed}}
	[[Image:3exh.png\|left\|200px]]		[[Image:3exh.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_3exh\| PDB=3exh \| SCENE= }}		{{STRUCTURE_3exh\| PDB=3exh \| SCENE= }}

	===Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex===		===Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex===

-
-	<!--
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	{{ABSTRACT_PUBMED_19081061}}		{{ABSTRACT_PUBMED_19081061}}

	==About this Structure==		==About this Structure==
-	~~3EXH~~ is a 8 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA].	+	[[3exh]] is a 8 chain structure of [[Pyruvate dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA].
		+
		+	==See Also==
		+	*[[Pyruvate dehydrogenase\|Pyruvate dehydrogenase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19081061~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019081061</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chuang, D T.]]		[[Category: Chuang, D T.]]
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	[[Category: Thiamine pyrophosphate]]		[[Category: Thiamine pyrophosphate]]
	[[Category: Transit peptide]]		[[Category: Transit peptide]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 18:52:37 2009''

OCA at 15:52, 10 June 2009

OCA — Wed, 10 Jun 2009 15:52:38 GMT

←Older revision		Revision as of 15:52, 10 June 2009
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	==About this Structure==		==About this Structure==
-	3EXH is a ~~[[Protein complex]]~~ structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA].	+	3EXH is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXH OCA].

	==Reference==		==Reference==
-	Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops., Kato M, Wynn RM, Chuang JL, Tso SC, Machius M, Li J, Chuang DT, Structure. 2008 Dec 12;16(12):1849-59. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/19081061 19081061]~~	+	<ref group="xtra">PMID:19081061</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: ~~Protein complex~~]]	+	[[Category: Chuang, D T.]]
-	[[Category: ~~Pdbx_ordinal=~~, ~~<PDBx~~:~~audit_author~~.]]	+	[[Category: Chuang, J L.]]
		+	[[Category: Kato, M.]]
		+	[[Category: Li, J.]]
		+	[[Category: Machius, M.]]
		+	[[Category: Tso, S C.]]
		+	[[Category: Wynn, R M.]]
	[[Category: Alternative splicing]]		[[Category: Alternative splicing]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
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	[[Category: Transit peptide]]		[[Category: Transit peptide]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jan 14 20~~:33:00 2009''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 18:52:37 2009''