1hti - Revision history

OCA at 07:30, 7 February 2024

OCA — Wed, 07 Feb 2024 07:30:16 GMT

←Older revision		Revision as of 07:30, 7 February 2024
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	<StructureSection load='1hti' size='340' side='right'caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1hti' size='340' side='right'caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1hti]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1hti]] is a 2 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=1HTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTI FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PGA:~~2~~-PHOSPHOGLYCOLIC+ACID'>PGA</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]] 2.8Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [https://pdbe.org/1hti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [https://www.ebi.ac.uk/pdbsum/1hti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hti 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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [https://pdbe.org/1hti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [https://www.ebi.ac.uk/pdbsum/1hti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hti ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN]] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[https://omim.org/entry/190450 190450]]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.	+	[https://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[https://omim.org/entry/190450 190450]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 22:
	</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=1hti 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=1hti ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The crystal structure of recombinant human triosephosphate isomerase (hTIM) has been determined complexed with the transition-state analogue 2-phosphoglycolate at a resolution of 2.8 A. After refinement, the R-factor is 16.7% with good geometry. The asymmetric unit contains 1 complete dimer of 53,000 Da, with only 1 of the subunits binding the inhibitor. The so-called flexible loop, comprising residues 168-174, is in its "closed" conformation in the subunit that binds the inhibitor, and in the "open" conformation in the other subunit. The tips of the loop in these 2 conformations differ up to 7 A in position. The RMS difference between hTIM and the enzyme of Trypanosoma brucei, the causative agent of sleeping sickness, is 1.12 A for 487 C alpha positions with 53% sequence identity. Significant sequence differences between the human and parasite enzymes occur at about 13 A from the phosphate binding site. The chicken and human enzymes have an RMS difference of 0.69 A for 484 equivalent residues and about 90% sequence identity. Complementary mutations ensure a great similarity in the packing of side chains in the core of the beta-barrels of these 2 enzymes. Three point mutations in hTIM have been correlated with severe genetic disorders ranging from hemolytic disorder to neuromuscular impairment. Knowledge of the structure of the human enzyme provides insight into the probable effect of 2 of these mutations, Glu 104 to Asp and Phe 240 to Ile, on the enzyme. The third mutation reported to be responsible for a genetic disorder, Gly 122 to Arg, is however difficult to explain. This residue is far away from both catalytic centers in the dimer, as well as from the dimer interface, and seems unlikely to affect stability or activity. Inspection of the 3-dimensional structure of trypanosomal triosephosphate isomerase, which has a methionine at position 122, only increased the mystery of the effects of the Gly to Arg mutation in the human enzyme.
-
-	Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme.,Mande SC, Mainfroid V, Kalk KH, Goraj K, Martial JA, Hol WG Protein Sci. 1994 May;3(5):810-21. PMID:8061610<ref>PMID:8061610</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1hti" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Triose phosphate isomerase 3D structures\|Triose phosphate isomerase 3D structures]]		*[[Triose phosphate isomerase 3D structures\|Triose phosphate isomerase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Triose-phosphate isomerase]]~~	+	[[Category: Hol WGJ]]
-	[[Category: Hol~~, W G.J~~]]	+	[[Category: Mande SC]]
-	[[Category: Mande~~, S C~~]]	+

OCA at 07:27, 7 April 2021

OCA — Wed, 07 Apr 2021 07:27:53 GMT

←Older revision		Revision as of 07:27, 7 April 2021
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	<StructureSection load='1hti' size='340' side='right'caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1hti' size='340' side='right'caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1hti]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTI OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1HTI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1hti]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTI FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [~~http~~://pdbe.org/1hti PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1hti PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1hti 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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [https://pdbe.org/1hti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [https://www.ebi.ac.uk/pdbsum/1hti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hti ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN]] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[~~http~~://omim.org/entry/190450 190450]]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.	+	[[https://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN]] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[https://omim.org/entry/190450 190450]]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Triose ~~Phosphate Isomerase~~\|Triose ~~Phosphate Isomerase~~]]	+	*[[Triose phosphate isomerase 3D structures\|Triose phosphate isomerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:38, 3 July 2019

OCA — Wed, 03 Jul 2019 07:38:45 GMT

←Older revision		Revision as of 07:38, 3 July 2019
Line 1:		Line 1:

	==CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME==		==CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME==
-	<StructureSection load='1hti' size='340' side='right' caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='1hti' size='340' side='right'caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1hti]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTI FirstGlance]. <br>		<table><tr><td colspan='2'>[[1hti]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTI FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/1hti_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/1hti_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 36:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]
	[[Category: Hol, W G.J]]		[[Category: Hol, W G.J]]
	[[Category: Mande, S C]]		[[Category: Mande, S C]]

OCA at 10:41, 27 September 2017

OCA — Wed, 27 Sep 2017 10:41:15 GMT

←Older revision		Revision as of 10:41, 27 September 2017
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME==		==CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME==
	<StructureSection load='1hti' size='340' side='right' caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1hti' size='340' side='right' caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1hti]] is a 2 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=1HTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1hti]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [http://pdbe.org/1hti PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [http://www.ebi.ac.uk/pdbsum/1hti 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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [http://pdbe.org/1hti PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [http://www.ebi.ac.uk/pdbsum/1hti PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hti ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 17:		Line 18:
	<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=1hti ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Human]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]
	[[Category: Hol, W G.J]]		[[Category: Hol, W G.J]]
	[[Category: Mande, S C]]		[[Category: Mande, S C]]

OCA at 23:14, 11 September 2015

OCA — Fri, 11 Sep 2015 23:14:07 GMT

←Older revision		Revision as of 23:14, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1hti' size='340' side='right' caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1hti' size='340' side='right' caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1hti]] is a 2 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=1HTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1hti]] is a 2 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=1HTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [http://www.ebi.ac.uk/pdbsum/1hti 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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [http://pdbe.org/1hti PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [http://www.ebi.ac.uk/pdbsum/1hti PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 27:		Line 27:
	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 1hti" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]
	[[Category: Hol, W G.J]]		[[Category: Hol, W G.J]]
	[[Category: Mande, S C]]		[[Category: Mande, S C]]

OCA at 20:42, 25 December 2014

OCA — Thu, 25 Dec 2014 20:42:28 GMT

←Older revision		Revision as of 20:42, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1hti]] is a 2 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=1HTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTI FirstGlance]. <br>		<table><tr><td colspan='2'>[[1hti]] is a 2 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=1HTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTI FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [http://www.ebi.ac.uk/pdbsum/1hti 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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [http://www.ebi.ac.uk/pdbsum/1hti PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN]] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[http://omim.org/entry/190450 190450]]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.		[[http://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN]] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[http://omim.org/entry/190450 190450]]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.
-	== Function ==
-
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 36:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]
-	[[Category: Hol, W G.J.]]	+	[[Category: Hol, W G.J]]
-	[[Category: Mande, S C.]]	+	[[Category: Mande, S C]]

OCA at 15:38, 29 September 2014

OCA — Mon, 29 Sep 2014 15:38:12 GMT

←Older revision		Revision as of 15:38, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1hti\| PDB=1hti \| SCENE= }}~~	+	==CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME==
-	===CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME===	+	<StructureSection load='1hti' size='340' side='right' caption='[[1hti]], [[Resolution\|resolution]] 2.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_8061610}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[1hti]] is a 2 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=1HTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTI FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=1hti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hti OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hti RCSB], [http://www.ebi.ac.uk/pdbsum/1hti PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN]] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[http://omim.org/entry/190450 190450]]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.		[[http://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN]] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[http://omim.org/entry/190450 190450]]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.
		+	== Function ==

-	==~~About this Structure~~==	+	== Evolutionary Conservation ==
-	[[~~1hti~~]] ~~is a 2 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=~~1HTI OCA~~].	+	[[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/ht/1hti_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 ==
		+	The crystal structure of recombinant human triosephosphate isomerase (hTIM) has been determined complexed with the transition-state analogue 2-phosphoglycolate at a resolution of 2.8 A. After refinement, the R-factor is 16.7% with good geometry. The asymmetric unit contains 1 complete dimer of 53,000 Da, with only 1 of the subunits binding the inhibitor. The so-called flexible loop, comprising residues 168-174, is in its "closed" conformation in the subunit that binds the inhibitor, and in the "open" conformation in the other subunit. The tips of the loop in these 2 conformations differ up to 7 A in position. The RMS difference between hTIM and the enzyme of Trypanosoma brucei, the causative agent of sleeping sickness, is 1.12 A for 487 C alpha positions with 53% sequence identity. Significant sequence differences between the human and parasite enzymes occur at about 13 A from the phosphate binding site. The chicken and human enzymes have an RMS difference of 0.69 A for 484 equivalent residues and about 90% sequence identity. Complementary mutations ensure a great similarity in the packing of side chains in the core of the beta-barrels of these 2 enzymes. Three point mutations in hTIM have been correlated with severe genetic disorders ranging from hemolytic disorder to neuromuscular impairment. Knowledge of the structure of the human enzyme provides insight into the probable effect of 2 of these mutations, Glu 104 to Asp and Phe 240 to Ile, on the enzyme. The third mutation reported to be responsible for a genetic disorder, Gly 122 to Arg, is however difficult to explain. This residue is far away from both catalytic centers in the dimer, as well as from the dimer interface, and seems unlikely to affect stability or activity. Inspection of the 3-dimensional structure of trypanosomal triosephosphate isomerase, which has a methionine at position 122, only increased the mystery of the effects of the Gly to Arg mutation in the human enzyme.
		+
		+	Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme.,Mande SC, Mainfroid V, Kalk KH, Goraj K, Martial JA, Hol WG Protein Sci. 1994 May;3(5):810-21. PMID:8061610<ref>PMID:8061610</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Triose Phosphate Isomerase\|Triose Phosphate Isomerase]]		*[[Triose Phosphate Isomerase\|Triose Phosphate Isomerase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:008061610</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]
	[[Category: Hol, W G.J.]]		[[Category: Hol, W G.J.]]
	[[Category: Mande, S C.]]		[[Category: Mande, S C.]]

OCA at 02:41, 25 March 2013

OCA — Mon, 25 Mar 2013 02:41:16 GMT

←Older revision		Revision as of 02:41, 25 March 2013
Line 2:		Line 2:
	===CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME===		===CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME===
	{{ABSTRACT_PUBMED_8061610}}		{{ABSTRACT_PUBMED_8061610}}
		+
		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN]] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[http://omim.org/entry/190450 190450]]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.

	==About this Structure==		==About this Structure==
Line 10:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:008061610</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008061610</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]
	[[Category: Hol, W G.J.]]		[[Category: Hol, W G.J.]]
	[[Category: Mande, S C.]]		[[Category: Mande, S C.]]

OCA at 11:03, 11 March 2013

OCA — Mon, 11 Mar 2013 11:03:49 GMT

←Older revision		Revision as of 11:03, 11 March 2013
Line 1:		Line 1:
-	[[Image:1hti.png\|left\|200px]]
-
	{{STRUCTURE_1hti\| PDB=1hti \| SCENE= }}		{{STRUCTURE_1hti\| PDB=1hti \| SCENE= }}
-
	===CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME===		===CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME===
-
	{{ABSTRACT_PUBMED_8061610}}		{{ABSTRACT_PUBMED_8061610}}

OCA at 21:23, 20 October 2012

OCA — Sat, 20 Oct 2012 21:23:28 GMT

←Older revision		Revision as of 21:23, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1hti]] is a 2 chain structure ~~of [[Triose Phosphate Isomerase]]~~ 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=1HTI OCA].	+	[[1hti]] is a 2 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=1HTI OCA].

	==See Also==		==See Also==
Line 14:		Line 14:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:008061610~~</ref><ref group="xtra">PMID:009285490~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008061610</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]
	[[Category: Hol, W G.J.]]		[[Category: Hol, W G.J.]]
	[[Category: Mande, S C.]]		[[Category: Mande, S C.]]