4gdx - Revision history

OCA at 15:44, 14 March 2024

OCA — Thu, 14 Mar 2024 15:44:14 GMT

←Older revision		Revision as of 15:44, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gdx]] 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=4GDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GDX FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gdx]] 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=4GDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GDX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.67Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4gdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdx OCA], [https://pdbe.org/4gdx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gdx RCSB], [https://www.ebi.ac.uk/pdbsum/4gdx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdx 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=4gdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdx OCA], [https://pdbe.org/4gdx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gdx RCSB], [https://www.ebi.ac.uk/pdbsum/4gdx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdx ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>		[https://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The enzyme gamma-glutamyl transpeptidase 1 (GGT1) is a conserved member of the Nterminal nucleophile (Ntn)-hydroylase family that cleaves the gamma-glutamyl bond of glutathione and other gamma-glutamyl compounds. In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status. Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer. The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model. The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs. We report the high-resolution (1.67 A) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT. Comparisons of the active site architecture of hGGT1 to those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme. Compared to several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site. The hGGT1 structure also revealed tightly bound chlorides near the catalytic residue that may contribute to catalytic activity. These are absent in the bacterial GGTs. These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.
-
-	Novel insights into eukaryotic gamma-glutamyl transpeptidase 1 from the crystal structure of the glutamate-bound human enzyme.,West MB, Chen Y, Wickham S, Heroux A, Cahill K, Hanigan MH, Mooers BH J Biol Chem. 2013 Sep 18. PMID:24047895<ref>PMID:24047895</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gdx" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:50, 26 October 2022

OCA — Wed, 26 Oct 2022 06:50:22 GMT

←Older revision		Revision as of 06:50, 26 October 2022
Line 1:		Line 1:

	==Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex==		==Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex==
-	<StructureSection load='4gdx' size='340' side='right' caption='[[4gdx]], [[Resolution\|resolution]] 1.67Å' scene=''>	+	<StructureSection load='4gdx' size='340' side='right'caption='[[4gdx]], [[Resolution\|resolution]] 1.67Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gdx]] 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=4GDX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GDX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gdx]] 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=4GDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GDX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dbu\|2dbu]], [[2eoy\|2eoy]], [[2eox\|2eox]], [[2eow\|2eow]], [[2dbx\|2dbx]], [[2nqo\|2nqo]], [[2dg5\|2dg5]], [[2dbw\|2dbw]], [[4gg2\|4gg2]], [[4gg3\|4gg3]]</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=4gdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdx OCA], [https://pdbe.org/4gdx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gdx RCSB], [https://www.ebi.ac.uk/pdbsum/4gdx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdx ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GGT, GGT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=4gdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdx OCA], [~~http~~://pdbe.org/4gdx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gdx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gdx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdx ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>	+	[https://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Cahill, K]]	+	[[Category: Large Structures]]
-	[[Category: Chen, Y]]	+	[[Category: Cahill K]]
-	[[Category: Hanigan~~, M H~~]]	+	[[Category: Chen Y]]
-	[[Category: Heroux, A]]	+	[[Category: Hanigan MH]]
-	[[Category: Mooers~~, B H.M~~]]	+	[[Category: Heroux A]]
-	[[Category: West~~, M B~~]]	+	[[Category: Mooers BHM]]
-	[[Category: Wickham, S]]	+	[[Category: West MB]]
-	~~[[Category: Cell surface]]~~	+	[[Category: Wickham S]]
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: N-glycosylation]]~~	+
-	~~[[Category: Ntn-hydrolase family]]~~	+
-	~~[[Category: Product-enzyme complex~~]]	+

OCA at 06:15, 5 August 2016

OCA — Fri, 05 Aug 2016 06:15:53 GMT

←Older revision		Revision as of 06:15, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex==		==Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex==
	<StructureSection load='4gdx' size='340' side='right' caption='[[4gdx]], [[Resolution\|resolution]] 1.67Å' scene=''>		<StructureSection load='4gdx' size='340' side='right' caption='[[4gdx]], [[Resolution\|resolution]] 1.67Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dbu\|2dbu]], [[2eoy\|2eoy]], [[2eox\|2eox]], [[2eow\|2eow]], [[2dbx\|2dbx]], [[2nqo\|2nqo]], [[2dg5\|2dg5]], [[2dbw\|2dbw]], [[4gg2\|4gg2]], [[4gg3\|4gg3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dbu\|2dbu]], [[2eoy\|2eoy]], [[2eox\|2eox]], [[2eow\|2eow]], [[2dbx\|2dbx]], [[2nqo\|2nqo]], [[2dg5\|2dg5]], [[2dbw\|2dbw]], [[4gg2\|4gg2]], [[4gg3\|4gg3]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GGT, GGT1 ([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">GGT, GGT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4gdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gdx RCSB], [http://www.ebi.ac.uk/pdbsum/4gdx 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=4gdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdx OCA], [http://pdbe.org/4gdx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gdx RCSB], [http://www.ebi.ac.uk/pdbsum/4gdx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdx ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	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 4gdx" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:24, 21 December 2014

OCA — Sun, 21 Dec 2014 17:24:33 GMT

←Older revision		Revision as of 17:24, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4gdx\| PDB=4gdx \| SCENE= }}~~	+	==Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex==
-	===Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex===	+	<StructureSection load='4gdx' size='340' side='right' caption='[[4gdx]], [[Resolution\|resolution]] 1.67Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24047895}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4gdx]] 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=4GDX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GDX FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dbu\|2dbu]], [[2eoy\|2eoy]], [[2eox\|2eox]], [[2eow\|2eow]], [[2dbx\|2dbx]], [[2nqo\|2nqo]], [[2dg5\|2dg5]], [[2dbw\|2dbw]], [[4gg2\|4gg2]], [[4gg3\|4gg3]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GGT, GGT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4gdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gdx RCSB], [http://www.ebi.ac.uk/pdbsum/4gdx PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.		[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>		[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The enzyme gamma-glutamyl transpeptidase 1 (GGT1) is a conserved member of the Nterminal nucleophile (Ntn)-hydroylase family that cleaves the gamma-glutamyl bond of glutathione and other gamma-glutamyl compounds. In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status. Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer. The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model. The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs. We report the high-resolution (1.67 A) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT. Comparisons of the active site architecture of hGGT1 to those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme. Compared to several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site. The hGGT1 structure also revealed tightly bound chlorides near the catalytic residue that may contribute to catalytic activity. These are absent in the bacterial GGTs. These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.

-	~~==About this Structure==~~	+	Novel insights into eukaryotic gamma-glutamyl transpeptidase 1 from the crystal structure of the glutamate-bound human enzyme.,West MB, Chen Y, Wickham S, Heroux A, Cahill K, Hanigan MH, Mooers BH J Biol Chem. 2013 Sep 18. PMID:24047895<ref>PMID:24047895</ref>
-	~~[[4gdx]] 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=4GDX OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024047895</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Cahill, K.]]	+	[[Category: Cahill, K]]
-	[[Category: Chen, Y.]]	+	[[Category: Chen, Y]]
-	[[Category: Hanigan, M H.]]	+	[[Category: Hanigan, M H]]
-	[[Category: Heroux, A.]]	+	[[Category: Heroux, A]]
-	[[Category: Mooers, B H.M.]]	+	[[Category: Mooers, B H.M]]
-	[[Category: West, M B.]]	+	[[Category: West, M B]]
-	[[Category: Wickham, S.]]	+	[[Category: Wickham, S]]
	[[Category: Cell surface]]		[[Category: Cell surface]]
	[[Category: Glycoprotein]]		[[Category: Glycoprotein]]

OCA at 08:30, 27 November 2013

OCA — Wed, 27 Nov 2013 08:30:34 GMT

←Older revision		Revision as of 08:30, 27 November 2013
Line 10:		Line 10:

	==About this Structure==		==About this Structure==
-	[[4gdx]] 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=4GDX OCA].	+	[[4gdx]] 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=4GDX OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:024047895</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:024047895</ref><references group="xtra"/><references/>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Cahill, K.]]		[[Category: Cahill, K.]]
	[[Category: Chen, Y.]]		[[Category: Chen, Y.]]

OCA at 06:45, 16 October 2013

OCA — Wed, 16 Oct 2013 06:45:51 GMT

←Older revision		Revision as of 06:45, 16 October 2013
Line 1:		Line 1:
	{{STRUCTURE_4gdx\| PDB=4gdx \| SCENE= }}		{{STRUCTURE_4gdx\| PDB=4gdx \| SCENE= }}
	===Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex===		===Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex===
		+	{{ABSTRACT_PUBMED_24047895}}

	==Disease==		==Disease==
Line 12:		Line 13:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024047895</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Cahill, K.]]		[[Category: Cahill, K.]]

OCA at 08:16, 29 September 2013

OCA — Sun, 29 Sep 2013 08:16:49 GMT

←Older revision		Revision as of 08:16, 29 September 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4gdx\| PDB=4gdx \| SCENE= }}
		+	===Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex===

-	The ~~entry 4gdx~~ is ~~ON HOLD until Sep 30 2014~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.

-	~~Authors~~: ~~West, M~~.B., ~~Chen, Y~~.~~, Wickham, S~~.~~, Heroux, A~~., ~~Cahill, K~~.~~, Hanigan, M.H., Mooers, B.H.M~~.	+	==Function==
		+	[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>

-	~~Description: Crystal~~ Structure ~~of Human Gamma~~-~~Glutamyl Transpeptidase~~--~~Glutamate~~ complex	+	==About this Structure==
		+	[[4gdx]] 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=4GDX OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Cahill, K.]]
		+	[[Category: Chen, Y.]]
		+	[[Category: Hanigan, M H.]]
		+	[[Category: Heroux, A.]]
		+	[[Category: Mooers, B H.M.]]
		+	[[Category: West, M B.]]
		+	[[Category: Wickham, S.]]
		+	[[Category: Cell surface]]
		+	[[Category: Glycoprotein]]
		+	[[Category: Hydrolase]]
		+	[[Category: N-glycosylation]]
		+	[[Category: Ntn-hydrolase family]]
		+	[[Category: Product-enzyme complex]]

OCA at 09:33, 4 September 2013

OCA — Wed, 04 Sep 2013 09:33:04 GMT

←Older revision		Revision as of 09:33, 4 September 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gdx is ON HOLD until ~~Paper Publication~~	+	The entry 4gdx is ON HOLD until Sep 30 2014

	Authors: West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H.M.		Authors: West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H.M.

	Description: Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex		Description: Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex

OCA at 13:40, 6 March 2013

OCA — Wed, 06 Mar 2013 13:40:19 GMT

←Older revision		Revision as of 13:40, 6 March 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gdx is ON HOLD until ~~sometime in the future~~	+	The entry 4gdx is ON HOLD until Paper Publication

	Authors: West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H.M.		Authors: West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H.M.

	Description: Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex		Description: Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex

OCA at 08:46, 2 January 2013

OCA — Wed, 02 Jan 2013 08:46:30 GMT

←Older revision		Revision as of 08:46, 2 January 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gdx is ON HOLD	+	The entry 4gdx is ON HOLD until sometime in the future

	Authors: West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H.M.		Authors: West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H.M.

	Description: Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex		Description: Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex