4gsz - Revision history

OCA at 15:55, 14 March 2024

2024-03-14T15:55:35Z

←Older revision		Revision as of 15:55, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gsz]] 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=4GSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GSZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gsz]] 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=4GSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GSZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4gsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsz OCA], [https://pdbe.org/4gsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gsz RCSB], [https://www.ebi.ac.uk/pdbsum/4gsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gsz 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=4gsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsz OCA], [https://pdbe.org/4gsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gsz RCSB], [https://www.ebi.ac.uk/pdbsum/4gsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gsz ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]		[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Various binuclear metal ion clusters and complexes have been reconstituted in crystalline human arginase I by removing the Mn(2+)(2) cluster of the wild-type enzyme with metal chelators and subsequently soaking the crystalline apoenzyme in buffer solutions containing NiCl(2) or ZnCl(2). X-ray crystal structures of these metal ion variants are correlated with catalytic activity measurements that reveal differences resulting from metal ion substitution. Additionally, treatment of crystalline Mn(2+)(2)-human arginase I with Zn(2+) reveals for the first time the structural basis for inhibition by Zn(2+), which forms a carboxylate-histidine-Zn(2+) triad with H141 and E277. The imidazole side chain of H141 is known to be hyper-reactive, and its chemical modification or mutagenesis is known to similarly compromise catalysis. The reactive substrate analogue 2(S)-amino-6-boronohexanoic acid (ABH) binds as a tetrahedral boronate anion to Mn(2+)(2), Co(2+)(2), Ni(2+)(2), and Zn(2+)(2) clusters in human arginase I, and it can be stabilized by a third inhibitory Zn(2+) ion coordinated by H141. Because ABH binds as an analogue of the tetrahedral intermediate and its flanking transition states in catalysis, this implies that the various metallo-substituted enzymes are capable of some level of catalysis with an actual substrate. Accordingly, we establish the following trend for turnover number (k(cat)) and catalytic efficiency (k(cat)/K(M)): Mn(2+) > Ni(2+) approximately Co(2+) >> Zn(2+). Therefore, Mn(2+) is required for optimal catalysis by human arginase I.
-
-	Structure and function of non-native metal clusters in human arginase I.,D'Antonio EL, Hai Y, Christianson DW Biochemistry. 2012 Oct 23;51(42):8399-409. doi: 10.1021/bi301145n. Epub 2012 Oct , 12. PMID:23061982<ref>PMID:23061982</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gsz" style="background-color:#fffaf0;"></div>

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

OCA at 07:15, 26 October 2022

2022-10-26T07:15:54Z

←Older revision		Revision as of 07:15, 26 October 2022
Line 1:		Line 1:

	==Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex==		==Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex==
-	<StructureSection load='4gsz' size='340' side='right' caption='[[4gsz]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='4gsz' size='340' side='right'caption='[[4gsz]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gsz]] 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=4GSZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GSZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gsz]] 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=4GSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GSZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2aeb\|2aeb]], [[3thh\|3thh]], [[4gsv\|4gsv]], [[4gsk\|4gsk]]</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=4gsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsz OCA], [https://pdbe.org/4gsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gsz RCSB], [https://www.ebi.ac.uk/pdbsum/4gsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gsz ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </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=4gsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsz OCA], [~~http~~://pdbe.org/4gsz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gsz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gsz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gsz ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[~~http~~://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>	+	[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[https://omim.org/entry/207800 207800]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 22:

	==See Also==		==See Also==
-	*[[Arginase\|Arginase]]	+	*[[Arginase 3D structures\|Arginase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Arginase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Antonio, E L.D~~]]	+	[[Category: Christianson DW]]
-	[[Category: ~~Christianson,~~ D W]]	+	[[Category: D'Antonio EL]]
-	[[Category: Hai, Y]]	+	[[Category: Hai Y]]
-	~~[[Category: Arginase fold]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex~~]]	+

OCA at 05:35, 5 August 2016

2016-08-05T05:35:22Z

←Older revision		Revision as of 05:35, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex==		==Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex==
	<StructureSection load='4gsz' size='340' side='right' caption='[[4gsz]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='4gsz' size='340' side='right' caption='[[4gsz]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gsz]] 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=4GSZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GSZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gsz]] 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=4GSZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GSZ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2aeb\|2aeb]], [[3thh\|3thh]], [[4gsv\|4gsv]], [[4gsk\|4gsk]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2aeb\|2aeb]], [[3thh\|3thh]], [[4gsv\|4gsv]], [[4gsk\|4gsk]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </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=4gsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gsz RCSB], [http://www.ebi.ac.uk/pdbsum/4gsz 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=4gsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsz OCA], [http://pdbe.org/4gsz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gsz RCSB], [http://www.ebi.ac.uk/pdbsum/4gsz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gsz ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	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 4gsz" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Arginase]]		[[Category: Arginase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Antonio, E L.D]]		[[Category: Antonio, E L.D]]
	[[Category: Christianson, D W]]		[[Category: Christianson, D W]]

OCA at 23:26, 24 December 2014

2014-12-24T23:26:23Z

←Older revision		Revision as of 23:26, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4gsz\| PDB=4gsz \| SCENE= }}~~	+	==Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex==
-	===Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex===	+	<StructureSection load='4gsz' size='340' side='right' caption='[[4gsz]], [[Resolution\|resolution]] 2.20Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23061982}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4gsz]] 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=4GSZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GSZ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2aeb\|2aeb]], [[3thh\|3thh]], [[4gsv\|4gsv]], [[4gsk\|4gsk]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </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=4gsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gsz RCSB], [http://www.ebi.ac.uk/pdbsum/4gsz PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[http://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Various binuclear metal ion clusters and complexes have been reconstituted in crystalline human arginase I by removing the Mn(2+)(2) cluster of the wild-type enzyme with metal chelators and subsequently soaking the crystalline apoenzyme in buffer solutions containing NiCl(2) or ZnCl(2). X-ray crystal structures of these metal ion variants are correlated with catalytic activity measurements that reveal differences resulting from metal ion substitution. Additionally, treatment of crystalline Mn(2+)(2)-human arginase I with Zn(2+) reveals for the first time the structural basis for inhibition by Zn(2+), which forms a carboxylate-histidine-Zn(2+) triad with H141 and E277. The imidazole side chain of H141 is known to be hyper-reactive, and its chemical modification or mutagenesis is known to similarly compromise catalysis. The reactive substrate analogue 2(S)-amino-6-boronohexanoic acid (ABH) binds as a tetrahedral boronate anion to Mn(2+)(2), Co(2+)(2), Ni(2+)(2), and Zn(2+)(2) clusters in human arginase I, and it can be stabilized by a third inhibitory Zn(2+) ion coordinated by H141. Because ABH binds as an analogue of the tetrahedral intermediate and its flanking transition states in catalysis, this implies that the various metallo-substituted enzymes are capable of some level of catalysis with an actual substrate. Accordingly, we establish the following trend for turnover number (k(cat)) and catalytic efficiency (k(cat)/K(M)): Mn(2+) > Ni(2+) approximately Co(2+) >> Zn(2+). Therefore, Mn(2+) is required for optimal catalysis by human arginase I.

-	~~==Disease==~~	+	Structure and function of non-native metal clusters in human arginase I.,D'Antonio EL, Hai Y, Christianson DW Biochemistry. 2012 Oct 23;51(42):8399-409. doi: 10.1021/bi301145n. Epub 2012 Oct , 12. PMID:23061982<ref>PMID:23061982</ref>
-	~~[[http://www~~.~~uniprot~~.~~org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia~~ (~~ARGIN~~) ~~[MIM~~:~~[http~~:~~//omim~~.~~org~~/~~entry/207800 207800]]; also known as hyperargininemia~~. ~~Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid~~, ~~and periodic hyperammonemia occurs~~. ~~Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>~~PMID:~~1463019</ref>~~<ref>PMID:~~7649538~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4gsz]] 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=4GSZ OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	<references ~~group="xtra"~~/><~~references~~/>	+	*[[Arginase\|Arginase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Arginase]]		[[Category: Arginase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Antonio, E L.D.]]	+	[[Category: Antonio, E L.D]]
-	[[Category: Christianson, D W.]]	+	[[Category: Christianson, D W]]
-	[[Category: Hai, Y.]]	+	[[Category: Hai, Y]]
	[[Category: Arginase fold]]		[[Category: Arginase fold]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA at 12:19, 24 March 2013

2013-03-24T12:19:24Z

←Older revision		Revision as of 12:19, 24 March 2013
Line 1:		Line 1:
-	[[Image:4gsz.png\|left\|200px]]
-
	{{STRUCTURE_4gsz\| PDB=4gsz \| SCENE= }}		{{STRUCTURE_4gsz\| PDB=4gsz \| SCENE= }}
-
	===Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex===		===Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex===
		+	{{ABSTRACT_PUBMED_23061982}}

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[http://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref><ref>PMID:7649538</ref>

	==About this Structure==		==About this Structure==
	[[4gsz]] 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=4GSZ OCA].		[[4gsz]] 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=4GSZ OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Arginase]]		[[Category: Arginase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 06:34, 14 November 2012

2012-11-14T06:34:48Z

←Older revision		Revision as of 06:34, 14 November 2012
Line 1:		Line 1:
-	[[Image:4gsz.~~jpg~~\|left\|200px]]	+	[[Image:4gsz.png\|left\|200px]]

	{{STRUCTURE_4gsz\| PDB=4gsz \| SCENE= }}		{{STRUCTURE_4gsz\| PDB=4gsz \| SCENE= }}

OCA at 20:51, 26 September 2012

2012-09-26T20:51:34Z

←Older revision		Revision as of 20:51, 26 September 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4gsz.jpg\|left\|200px]]

-	~~The entry~~ 4gsz ~~is ON HOLD~~	+	{{STRUCTURE_4gsz\| PDB=4gsz \| SCENE= }}

-	~~Authors: D'Antonio, E.L., Hai, Y., Christianson, D.W.~~	+	===Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex===

-	~~Description: Crystal~~ Structure ~~of the Zn2+5~~-~~Human~~ Arginase I-~~ABH Complex~~	+
		+	==About this Structure==
		+	[[4gsz]] 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=4GSZ OCA].
		+	[[Category: Arginase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Antonio, E L.D.]]
		+	[[Category: Christianson, D W.]]
		+	[[Category: Hai, Y.]]
		+	[[Category: Arginase fold]]
		+	[[Category: Hydrolase]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA: Protected "4gsz" [edit=sysop:move=sysop]

2012-09-05T04:58:17Z

Protected "4gsz" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:58, 5 September 2012

OCA: New page: '''Unreleased structure''' The entry 4gsz is ON HOLD Authors: D'Antonio, E.L., Hai, Y., Christianson, D.W. Description: Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex

2012-09-05T04:58:16Z

New page: '''Unreleased structure''' The entry 4gsz is ON HOLD Authors: D'Antonio, E.L., Hai, Y., Christianson, D.W. Description: Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex

New page

'''Unreleased structure'''

The entry 4gsz is ON HOLD

Authors: D'Antonio, E.L., Hai, Y., Christianson, D.W.

Description: Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex