3u96 - Revision history

OCA at 08:38, 20 March 2024

OCA — Wed, 20 Mar 2024 08:38:20 GMT

←Older revision		Revision as of 08:38, 20 March 2024
Line 3:		Line 3:
	<StructureSection load='3u96' size='340' side='right'caption='[[3u96]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3u96' size='340' side='right'caption='[[3u96]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3u96]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U96 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3u96]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U96 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CSN:N,4~~-~~DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>~~, ~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>yop51, yopH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~630~~ "~~Bacterium enterocoliticum~~" ~~Schleifstein and Coleman 1939])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSN:N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48]~~ </~~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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [https://pdbe.org/3u96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [https://www.ebi.ac.uk/pdbsum/3u96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u96 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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [https://pdbe.org/3u96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [https://www.ebi.ac.uk/pdbsum/3u96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u96 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/YOPH_YEREN YOPH_YEREN]] Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages.	+	[https://www.uniprot.org/uniprot/YOPH_YEREN YOPH_YEREN] Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Yersinia protein tyrosine phosphatase (YopH) is the most efficient enzyme among all PTPases. YopH is hyperactive compared to human PTPases, interfering with mammalian cellular pathways to achieve the pathogenicity of Yersinia. Two properties related to the catalytic loop structure differences have been proposed to affect its dynamics and enzyme efficiency. One is the ability of the loop to form stabilizing interactions to bound ligand after loop closure, which has long been recognized. In addition, the loop flexibility/mobility was suggested in a previous study to be a factor as well, based on the observation that incremental changes in PTPase loop structure by single point mutations to alanine often induce incremental changes in enzyme catalytic efficiency. In this study, the temperature jump relaxation spectroscopy (T-jump) has been used to discern the subtle changes of the loop dynamics due to point loop mutations. As expected, our results suggest a correlation between loop dynamics and the size of the residue on the catalytic loop. The stabilization of the enzyme-ligand complex is often enthalpy driven, achieved by formation of additional favorable hydrogen bonding/ionic interactions after loop closure. Interestingly, our T-jump and X-ray crystallography studies on YopH suggest that the elimination of some ligand-protein interactions by mutation does not necessarily destabilize the ligand-enzyme complex after loop closure, since the increased entropy in the forms of more mobile protein residues may be sufficient to compensate the free energy loss due to lost interactions and may even lead to enhanced efficiency of the enzyme catalysis. How these competing loop properties may affect loop dynamics and enzyme function are discussed.	+
-		+
-	Investigation of catalytic loop structure, dynamics, and function relationship of Yersinia protein tyrosine phosphatase by temperature-jump relaxation spectroscopy and X-ray structural determination.,Ke S, Ho MC, Zhadin N, Deng H, Callender R J Phys Chem B. 2012 May 31;116(21):6166-76. Epub 2012 May 22. PMID:22564106<ref>PMID:22564106</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3u96" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Tyrosine phosphatase 3D structures\|Tyrosine phosphatase 3D structures]]		*[[Tyrosine phosphatase 3D structures\|Tyrosine phosphatase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Protein-tyrosine-phosphatase~~]]	+	[[Category: Yersinia enterocolitica]]
-	[[Category: Ho~~, M C~~]]	+	[[Category: Ho MC]]
-	[[Category: Ke, S]]	+	[[Category: Ke S]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Ptpase]]~~	+
-	~~[[Category: Yoph~~]]	+

OCA at 06:03, 13 July 2022

OCA — Wed, 13 Jul 2022 06:03:21 GMT

←Older revision		Revision as of 06:03, 13 July 2022
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	==Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS==		==Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS==
-	<StructureSection load='3u96' size='340' side='right' caption='[[3u96]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='3u96' size='340' side='right'caption='[[3u96]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3u96]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3U96 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3u96]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U96 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSN:N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSN:N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">yop51, yopH ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 "Bacterium enterocoliticum" Schleifstein and Coleman 1939])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">yop51, yopH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 "Bacterium enterocoliticum" Schleifstein and Coleman 1939])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [~~http~~://pdbe.org/3u96 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3u96 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3u96 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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [https://pdbe.org/3u96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [https://www.ebi.ac.uk/pdbsum/3u96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u96 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/YOPH_YEREN YOPH_YEREN]] Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages.	+	[[https://www.uniprot.org/uniprot/YOPH_YEREN YOPH_YEREN]] Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 3u96" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3u96" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Tyrosine phosphatase 3D structures\|Tyrosine phosphatase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 25:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]		[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]
		+	[[Category: Large Structures]]
	[[Category: Protein-tyrosine-phosphatase]]		[[Category: Protein-tyrosine-phosphatase]]
	[[Category: Ho, M C]]		[[Category: Ho, M C]]

OCA at 10:01, 8 November 2017

OCA — Wed, 08 Nov 2017 10:01:13 GMT

←Older revision		Revision as of 10:01, 8 November 2017
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 3u96" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3u96" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Tyrosine phosphatase\|Tyrosine phosphatase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:48, 4 August 2016

OCA — Thu, 04 Aug 2016 18:48:31 GMT

←Older revision		Revision as of 18:48, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS==		==Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS==
	<StructureSection load='3u96' size='340' side='right' caption='[[3u96]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3u96' size='340' side='right' caption='[[3u96]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3u96]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Yersinia_enterocolitica Yersinia enterocolitica~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U96 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3u96]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U96 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSN:N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSN:N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">yop51, yopH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 ~~Yersinia enterocolitica~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">yop51, yopH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 "Bacterium enterocoliticum" Schleifstein and Coleman 1939])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [http://www.ebi.ac.uk/pdbsum/3u96 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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [http://pdbe.org/3u96 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [http://www.ebi.ac.uk/pdbsum/3u96 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u96 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 3u96" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]
	[[Category: Protein-tyrosine-phosphatase]]		[[Category: Protein-tyrosine-phosphatase]]
-	[[Category: Yersinia enterocolitica]]
	[[Category: Ho, M C]]		[[Category: Ho, M C]]
	[[Category: Ke, S]]		[[Category: Ke, S]]

OCA at 12:06, 25 December 2014

OCA — Thu, 25 Dec 2014 12:06:06 GMT

←Older revision		Revision as of 12:06, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3u96]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U96 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3u96]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U96 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSN:N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSN:N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">yop51, yopH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 Yersinia enterocolitica])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">yop51, yopH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 Yersinia enterocolitica])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [http://www.ebi.ac.uk/pdbsum/3u96 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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [http://www.ebi.ac.uk/pdbsum/3u96 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/YOPH_YEREN YOPH_YEREN]] Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 27:
	[[Category: Protein-tyrosine-phosphatase]]		[[Category: Protein-tyrosine-phosphatase]]
	[[Category: Yersinia enterocolitica]]		[[Category: Yersinia enterocolitica]]
-	[[Category: Ho, M C.]]	+	[[Category: Ho, M C]]
-	[[Category: Ke, S.]]	+	[[Category: Ke, S]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Ptpase]]		[[Category: Ptpase]]
	[[Category: Yoph]]		[[Category: Yoph]]

OCA at 09:18, 11 June 2014

OCA — Wed, 11 Jun 2014 09:18:57 GMT

←Older revision		Revision as of 09:18, 11 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3u96.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS==
		+	<StructureSection load='3u96' size='340' side='right' caption='[[3u96]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3u96]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U96 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSN:N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM'>CSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">yop51, yopH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 Yersinia enterocolitica])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=3u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u96 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u96 RCSB], [http://www.ebi.ac.uk/pdbsum/3u96 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Yersinia protein tyrosine phosphatase (YopH) is the most efficient enzyme among all PTPases. YopH is hyperactive compared to human PTPases, interfering with mammalian cellular pathways to achieve the pathogenicity of Yersinia. Two properties related to the catalytic loop structure differences have been proposed to affect its dynamics and enzyme efficiency. One is the ability of the loop to form stabilizing interactions to bound ligand after loop closure, which has long been recognized. In addition, the loop flexibility/mobility was suggested in a previous study to be a factor as well, based on the observation that incremental changes in PTPase loop structure by single point mutations to alanine often induce incremental changes in enzyme catalytic efficiency. In this study, the temperature jump relaxation spectroscopy (T-jump) has been used to discern the subtle changes of the loop dynamics due to point loop mutations. As expected, our results suggest a correlation between loop dynamics and the size of the residue on the catalytic loop. The stabilization of the enzyme-ligand complex is often enthalpy driven, achieved by formation of additional favorable hydrogen bonding/ionic interactions after loop closure. Interestingly, our T-jump and X-ray crystallography studies on YopH suggest that the elimination of some ligand-protein interactions by mutation does not necessarily destabilize the ligand-enzyme complex after loop closure, since the increased entropy in the forms of more mobile protein residues may be sufficient to compensate the free energy loss due to lost interactions and may even lead to enhanced efficiency of the enzyme catalysis. How these competing loop properties may affect loop dynamics and enzyme function are discussed.

-	~~{{STRUCTURE_3u96\| PDB=3u96 \| SCENE= }}~~	+	Investigation of catalytic loop structure, dynamics, and function relationship of Yersinia protein tyrosine phosphatase by temperature-jump relaxation spectroscopy and X-ray structural determination.,Ke S, Ho MC, Zhadin N, Deng H, Callender R J Phys Chem B. 2012 May 31;116(21):6166-76. Epub 2012 May 22. PMID:22564106<ref>PMID:22564106</ref>

-	~~===Crystal Structure of YopHQ357F(Catalytic Domain~~, ~~Residues 163-468) in complex with pNCS===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_22564106}}~~	+	==See Also==
-		+	*[[Tyrosine phosphatase\|Tyrosine phosphatase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~3u96~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:022564106<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Protein-tyrosine-phosphatase]]		[[Category: Protein-tyrosine-phosphatase]]
	[[Category: Yersinia enterocolitica]]		[[Category: Yersinia enterocolitica]]

OCA at 05:05, 29 August 2012

OCA — Wed, 29 Aug 2012 05:05:30 GMT

←Older revision		Revision as of 05:05, 29 August 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3u96.jpg\|left\|200px]]

-	~~The entry~~ 3u96 ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_3u96\| PDB=3u96 \| SCENE= }}

-	~~Authors: Ho~~, ~~M.C., Ke, S.~~	+	===Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS===

-	~~Description: Crystal~~ Structure ~~of YopHQ357F(Catalytic Domain, Residues 163-468) in complex~~ with ~~pNCS~~	+	{{ABSTRACT_PUBMED_22564106}}
		+
		+	==About this Structure==
		+	[[3u96]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U96 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022564106</ref><references group="xtra"/>
		+	[[Category: Protein-tyrosine-phosphatase]]
		+	[[Category: Yersinia enterocolitica]]
		+	[[Category: Ho, M C.]]
		+	[[Category: Ke, S.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Ptpase]]
		+	[[Category: Yoph]]

OCA at 07:33, 7 December 2011

OCA — Wed, 07 Dec 2011 07:33:56 GMT

←Older revision		Revision as of 07:33, 7 December 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3u96 is ON HOLD	+	The entry 3u96 is ON HOLD until Paper Publication

	Authors: Ho, M.C., Ke, S.		Authors: Ho, M.C., Ke, S.

	Description: Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS		Description: Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS

OCA: Protected "3u96" [edit=sysop:move=sysop]

OCA — Sun, 30 Oct 2011 08:55:40 GMT

Protected "3u96" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:55, 30 October 2011

OCA: New page: '''Unreleased structure''' The entry 3u96 is ON HOLD Authors: Ho, M.C., Ke, S. Description: Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS

OCA — Sun, 30 Oct 2011 08:55:39 GMT

New page: '''Unreleased structure''' The entry 3u96 is ON HOLD Authors: Ho, M.C., Ke, S. Description: Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS

New page

'''Unreleased structure'''

The entry 3u96 is ON HOLD

Authors: Ho, M.C., Ke, S.

Description: Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS