1egd - Revision history

OCA at 07:02, 7 February 2024

OCA — Wed, 07 Feb 2024 07:02:32 GMT

←Older revision		Revision as of 07:02, 7 February 2024
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	<StructureSection load='1egd' size='340' side='right'caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1egd' size='340' side='right'caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGD FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FAD:FLAVIN~~-~~ADENINE+DINUCLEOTIDE'>FAD</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]] 2.4Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [https://pdbe.org/1egd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [https://www.ebi.ac.uk/pdbsum/1egd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egd 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=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [https://pdbe.org/1egd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [https://www.ebi.ac.uk/pdbsum/1egd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[https://omim.org/entry/201450 201450]]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref> <ref>PMID:2394825</ref> <ref>PMID:2251268</ref> <ref>PMID:1684086</ref> <ref>PMID:1902818</ref> <ref>PMID:1671131</ref> <ref>PMID:8198141</ref> <ref>PMID:7603790</ref> <ref>PMID:7929823</ref> <ref>PMID:9158144</ref> <ref>PMID:9882619</ref> <ref>PMID:10767181</ref> <ref>PMID:11349232</ref> <ref>PMID:11409868</ref> <ref>PMID:11486912</ref>	+	[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[https://omim.org/entry/201450 201450]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref> <ref>PMID:2394825</ref> <ref>PMID:2251268</ref> <ref>PMID:1684086</ref> <ref>PMID:1902818</ref> <ref>PMID:1671131</ref> <ref>PMID:8198141</ref> <ref>PMID:7603790</ref> <ref>PMID:7929823</ref> <ref>PMID:9158144</ref> <ref>PMID:9882619</ref> <ref>PMID:10767181</ref> <ref>PMID:11349232</ref> <ref>PMID:11409868</ref> <ref>PMID:11486912</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] This enzyme is specific for acyl chain lengths of 4 to 16.	+	[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN] This enzyme is specific for acyl chain lengths of 4 to 16.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1egd 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=1egd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Crystal structures of the wild type human medium-chain acyl-CoA dehydrogenase (MCADH) and a double mutant in which its active center base-arrangement has been altered to that of long chain acyl-CoA dehydrogenase (LCADH), Glu376Gly/Thr255Glu, have been determined by X-ray crystallography at 2.75 and 2.4 A resolution, respectively. The catalytic base responsible for the alpha-proton abstraction from the thioester substrate is Glu376 in MCADH, while that in LCADH is Glu255 (MCADH numbering), located over 100 residues away in its primary amino acid sequence. The structures of the mutant complexed with C8-, C12, and C14-CoA have also been determined. The human enzyme structure is essentially the same as that of the pig enzyme. The structure of the mutant is unchanged upon ligand binding except for the conformations of a few side chains in the active site cavity. The substrate with chain length longer than C12 binds to the enzyme in multiple conformations at its omega-end. Glu255 has two conformations, "active" and "resting" forms, with the latter apparently stabilized by forming a hydrogen bond with Glu99. Both the direction in which Glu255 approaches the C alpha atom of the substrate and the distance between the Glu255 carboxylate and the C alpha atom are different from those of Glu376; these factors are responsible for the intrinsic differences in the kinetic properties as well as the substrate specificity. Solvent accessible space at the "midsection" of the active site cavity, where the C alpha-C beta bond of the thioester substrate and the isoalloxazine ring of the FAD are located, is larger in the mutant than in the wild type enzyme, implying greater O2 accessibility in the mutant which might account for the higher oxygen reactivity.
-
-	Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.,Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ Biochemistry. 1996 Sep 24;35(38):12412-20. PMID:8823176<ref>PMID:8823176</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1egd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Oxidoreductase]]~~	+	[[Category: Ghisla S]]
-	[[Category: Ghisla, S]]	+	[[Category: Kim JP]]
-	[[Category: Kim~~, J P~~]]	+	[[Category: Lee HJ]]
-	[[Category: Lee~~, H J~~]]	+	[[Category: Nandy A]]
-	[[Category: Nandy, A]]	+	[[Category: Paschke R]]
-	[[Category: Paschke, R]]	+	[[Category: Wang M]]
-	[[Category: Wang, M]]	+
-	~~[[Category: Acyl-coa dehydrogenase]]~~	+
-	~~[[Category: Electron transfer]]~~	+
-	~~[[Category: Flavoprotein~~]]	+

OCA at 09:37, 21 July 2021

OCA — Wed, 21 Jul 2021 09:37:04 GMT

OCA at 14:03, 16 October 2019

OCA — Wed, 16 Oct 2019 14:03:12 GMT

←Older revision		Revision as of 14:03, 16 October 2019
Line 1:		Line 1:

	==STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE==		==STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE==
-	<StructureSection load='1egd' size='340' side='right' caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='1egd' size='340' side='right'caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EGD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EGD FirstGlance]. <br>
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1egd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1egd" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Acyl-CoA dehydrogenase 3D structures\|Acyl-CoA dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Ghisla, S]]		[[Category: Ghisla, S]]

OCA at 07:13, 20 December 2017

OCA — Wed, 20 Dec 2017 07:13:24 GMT

←Older revision		Revision as of 07:13, 20 December 2017
Line 1:		Line 1:
		+
	==STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE==		==STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE==
	<StructureSection load='1egd' size='340' side='right' caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1egd' size='340' side='right' caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9] </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=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [http://pdbe.org/1egd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [http://www.ebi.ac.uk/pdbsum/1egd 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=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [http://pdbe.org/1egd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [http://www.ebi.ac.uk/pdbsum/1egd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1egd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1egd_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1egd_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>
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	</div>		</div>
	<div class="pdbe-citations 1egd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1egd" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Acyl-CoA dehydrogenase\|Acyl-CoA dehydrogenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:23, 8 February 2016

OCA — Mon, 08 Feb 2016 17:23:02 GMT

←Older revision		Revision as of 17:23, 8 February 2016
Line 19:		Line 19:
	<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=1egd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 13:47, 10 September 2015

OCA — Thu, 10 Sep 2015 13:47:15 GMT

←Older revision		Revision as of 13:47, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1egd' size='340' side='right' caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1egd' size='340' side='right' caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EGD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EGD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9] </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=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [http://www.ebi.ac.uk/pdbsum/1egd 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=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [http://pdbe.org/1egd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [http://www.ebi.ac.uk/pdbsum/1egd PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	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 1egd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Ghisla, S]]		[[Category: Ghisla, S]]

OCA at 22:19, 22 December 2014

OCA — Mon, 22 Dec 2014 22:19:57 GMT

←Older revision		Revision as of 22:19, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EGD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EGD FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [http://www.ebi.ac.uk/pdbsum/1egd 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=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [http://www.ebi.ac.uk/pdbsum/1egd PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[http://omim.org/entry/201450 201450]]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref> <ref>PMID:2394825</ref> <ref>PMID:2251268</ref> <ref>PMID:1684086</ref> <ref>PMID:1902818</ref> <ref>PMID:1671131</ref> <ref>PMID:8198141</ref> <ref>PMID:7603790</ref> <ref>PMID:7929823</ref> <ref>PMID:9158144</ref> <ref>PMID:9882619</ref> <ref>PMID:10767181</ref> <ref>PMID:11349232</ref> <ref>PMID:11409868</ref> <ref>PMID:11486912</ref>		[[http://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[http://omim.org/entry/201450 201450]]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref> <ref>PMID:2394825</ref> <ref>PMID:2251268</ref> <ref>PMID:1684086</ref> <ref>PMID:1902818</ref> <ref>PMID:1671131</ref> <ref>PMID:8198141</ref> <ref>PMID:7603790</ref> <ref>PMID:7929823</ref> <ref>PMID:9158144</ref> <ref>PMID:9882619</ref> <ref>PMID:10767181</ref> <ref>PMID:11349232</ref> <ref>PMID:11409868</ref> <ref>PMID:11486912</ref>
Line 38:		Line 38:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
-	[[Category: Ghisla, S.]]	+	[[Category: Ghisla, S]]
-	[[Category: Kim, J P.]]	+	[[Category: Kim, J P]]
-	[[Category: Lee, H J.]]	+	[[Category: Lee, H J]]
-	[[Category: Nandy, A.]]	+	[[Category: Nandy, A]]
-	[[Category: Paschke, R.]]	+	[[Category: Paschke, R]]
-	[[Category: Wang, M.]]	+	[[Category: Wang, M]]
	[[Category: Acyl-coa dehydrogenase]]		[[Category: Acyl-coa dehydrogenase]]
	[[Category: Electron transfer]]		[[Category: Electron transfer]]
	[[Category: Flavoprotein]]		[[Category: Flavoprotein]]

OCA at 16:10, 29 September 2014

OCA — Mon, 29 Sep 2014 16:10:40 GMT

←Older revision		Revision as of 16:10, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1egd\| PDB=1egd \| SCENE= }}~~	+	==STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE==
-	===STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE===	+	<StructureSection load='1egd' size='340' side='right' caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>
-	~~{{ABSTRACT_PUBMED_8823176}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EGD FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [http://www.ebi.ac.uk/pdbsum/1egd PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[http://omim.org/entry/201450 201450]]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref> <ref>PMID:2394825</ref> <ref>PMID:2251268</ref> <ref>PMID:1684086</ref> <ref>PMID:1902818</ref> <ref>PMID:1671131</ref> <ref>PMID:8198141</ref> <ref>PMID:7603790</ref> <ref>PMID:7929823</ref> <ref>PMID:9158144</ref> <ref>PMID:9882619</ref> <ref>PMID:10767181</ref> <ref>PMID:11349232</ref> <ref>PMID:11409868</ref> <ref>PMID:11486912</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] This enzyme is specific for acyl chain lengths of 4 to 16.
		+	== 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/eg/1egd_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 ==
		+	Crystal structures of the wild type human medium-chain acyl-CoA dehydrogenase (MCADH) and a double mutant in which its active center base-arrangement has been altered to that of long chain acyl-CoA dehydrogenase (LCADH), Glu376Gly/Thr255Glu, have been determined by X-ray crystallography at 2.75 and 2.4 A resolution, respectively. The catalytic base responsible for the alpha-proton abstraction from the thioester substrate is Glu376 in MCADH, while that in LCADH is Glu255 (MCADH numbering), located over 100 residues away in its primary amino acid sequence. The structures of the mutant complexed with C8-, C12, and C14-CoA have also been determined. The human enzyme structure is essentially the same as that of the pig enzyme. The structure of the mutant is unchanged upon ligand binding except for the conformations of a few side chains in the active site cavity. The substrate with chain length longer than C12 binds to the enzyme in multiple conformations at its omega-end. Glu255 has two conformations, "active" and "resting" forms, with the latter apparently stabilized by forming a hydrogen bond with Glu99. Both the direction in which Glu255 approaches the C alpha atom of the substrate and the distance between the Glu255 carboxylate and the C alpha atom are different from those of Glu376; these factors are responsible for the intrinsic differences in the kinetic properties as well as the substrate specificity. Solvent accessible space at the "midsection" of the active site cavity, where the C alpha-C beta bond of the thioester substrate and the isoalloxazine ring of the FAD are located, is larger in the mutant than in the wild type enzyme, implying greater O2 accessibility in the mutant which might account for the higher oxygen reactivity.

-	~~==Disease==~~	+	Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.,Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ Biochemistry. 1996 Sep 24;35(38):12412-20. PMID:8823176<ref>PMID:8823176</ref>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause~~ of acyl-CoA dehydrogenase ~~medium-chain deficiency (ACADMD) [MIM~~:~~[http://omim.org/entry/201450 201450]]~~. ~~It is an autosomal recessive disease which causes fasting hypoglycemia~~, ~~hepatic dysfunction~~, ~~and encephalopathy~~, ~~often resulting in death in infancy~~.~~<ref>PMID~~:~~2393404</ref><ref>~~PMID:2394825</ref><ref>PMID:2251268</ref><ref>PMID:1684086</ref><ref>PMID:1902818</ref><ref>PMID:1671131</ref><ref>PMID:8198141</ref><ref>PMID:7603790</ref><ref>PMID:7929823</ref><ref>PMID:9158144</ref><ref>PMID:9882619</ref><ref>PMID:10767181</ref><ref>PMID:11349232</ref><ref>PMID:11409868</ref><ref>PMID:~~11486912~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/ACADM_HUMAN ACADM_HUMAN]] This enzyme is specific for acyl chain lengths~~ of ~~4 to 16~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[1egd]] is a 4 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=1EGD OCA].~~	+

	==See Also==		==See Also==
	*[[Acyl-CoA dehydrogenase\|Acyl-CoA dehydrogenase]]		*[[Acyl-CoA dehydrogenase\|Acyl-CoA dehydrogenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:008823176</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 19:01, 24 March 2013

OCA — Sun, 24 Mar 2013 19:01:59 GMT

←Older revision		Revision as of 19:01, 24 March 2013
Line 1:		Line 1:
-	[[Image:1egd.png\|left\|200px]]
-
	{{STRUCTURE_1egd\| PDB=1egd \| SCENE= }}		{{STRUCTURE_1egd\| PDB=1egd \| SCENE= }}
-
	===STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE===		===STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE===
		+	{{ABSTRACT_PUBMED_8823176}}

-	~~{{ABSTRACT_PUBMED_8823176}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[http://omim.org/entry/201450 201450]]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref><ref>PMID:2394825</ref><ref>PMID:2251268</ref><ref>PMID:1684086</ref><ref>PMID:1902818</ref><ref>PMID:1671131</ref><ref>PMID:8198141</ref><ref>PMID:7603790</ref><ref>PMID:7929823</ref><ref>PMID:9158144</ref><ref>PMID:9882619</ref><ref>PMID:10767181</ref><ref>PMID:11349232</ref><ref>PMID:11409868</ref><ref>PMID:11486912</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] This enzyme is specific for acyl chain lengths of 4 to 16.

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:008823176</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008823176</ref><references group="xtra"/><references/>
-	~~[[Category: Acyl-CoA dehydrogenase]]~~	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Oxidoreductase]]
	[[Category: Ghisla, S.]]		[[Category: Ghisla, S.]]
	[[Category: Kim, J P.]]		[[Category: Kim, J P.]]

OCA at 10:53, 20 October 2012

OCA — Sat, 20 Oct 2012 10:53:26 GMT

←Older revision		Revision as of 10:53, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1egd]] is a 4 chain structure ~~of [[Acyl-CoA 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=1EGD OCA].	+	[[1egd]] is a 4 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=1EGD OCA].

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

←Older revision		Revision as of 09:37, 21 July 2021
Line 3:		Line 3:
	<StructureSection load='1egd' size='340' side='right'caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1egd' size='340' side='right'caption='[[1egd]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1EGD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1egd]] is a 4 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=1EGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9] </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=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [~~http~~://pdbe.org/1egd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1egd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1egd 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=1egd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egd OCA], [https://pdbe.org/1egd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egd RCSB], [https://www.ebi.ac.uk/pdbsum/1egd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[~~http~~://omim.org/entry/201450 201450]]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref> <ref>PMID:2394825</ref> <ref>PMID:2251268</ref> <ref>PMID:1684086</ref> <ref>PMID:1902818</ref> <ref>PMID:1671131</ref> <ref>PMID:8198141</ref> <ref>PMID:7603790</ref> <ref>PMID:7929823</ref> <ref>PMID:9158144</ref> <ref>PMID:9882619</ref> <ref>PMID:10767181</ref> <ref>PMID:11349232</ref> <ref>PMID:11409868</ref> <ref>PMID:11486912</ref>	+	[[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[https://omim.org/entry/201450 201450]]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref> <ref>PMID:2394825</ref> <ref>PMID:2251268</ref> <ref>PMID:1684086</ref> <ref>PMID:1902818</ref> <ref>PMID:1671131</ref> <ref>PMID:8198141</ref> <ref>PMID:7603790</ref> <ref>PMID:7929823</ref> <ref>PMID:9158144</ref> <ref>PMID:9882619</ref> <ref>PMID:10767181</ref> <ref>PMID:11349232</ref> <ref>PMID:11409868</ref> <ref>PMID:11486912</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] This enzyme is specific for acyl chain lengths of 4 to 16.	+	[[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] This enzyme is specific for acyl chain lengths of 4 to 16.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]