2h2u - Revision history

OCA at 09:51, 30 August 2023

2023-08-30T09:51:20Z

←Older revision		Revision as of 09:51, 30 August 2023
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	<StructureSection load='2h2u' size='340' side='right'caption='[[2h2u]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2h2u' size='340' side='right'caption='[[2h2u]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2h2u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H2U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2h2u]] 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=2H2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H2U FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.4Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;'>[[2h2n\|2h2n]]~~, [[~~1s18~~\|~~1s18~~]]~~, [[1s1d\|1s1d]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>CANT1, SHAPY ([https://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~~'>~~[https://en.wikipedia.org/wiki/Nucleoside_diphosphate_phosphatase Nucleoside diphosphate phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6]~~ </~~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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [https://pdbe.org/2h2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [https://www.ebi.ac.uk/pdbsum/2h2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2u 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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [https://pdbe.org/2h2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [https://www.ebi.ac.uk/pdbsum/2h2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2u ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN]] Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN] Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN]] Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.<ref>PMID:12234496</ref> <ref>PMID:15248776</ref> <ref>PMID:22539336</ref>	+	[https://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN] Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.<ref>PMID:12234496</ref> <ref>PMID:15248776</ref> <ref>PMID:22539336</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 37:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Nucleoside diphosphate phosphatase]]~~	+	[[Category: Herr AB]]
-	[[Category: Herr~~, A B~~]]	+	[[Category: Horii K]]
-	[[Category: Horii, K]]	+	[[Category: Kirley TL]]
-	[[Category: Kirley~~, T L~~]]	+	[[Category: Yang M]]
-	[[Category: Yang, M]]	+
-	~~[[Category: Calcium-binding protein]]~~	+
-	~~[[Category: Five-blade beta propeller]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Nucleotidase]]~~	+
-	~~[[Category: Nucleotide-binding~~]]	+

OCA at 07:30, 17 March 2021

2021-03-17T07:30:01Z

←Older revision		Revision as of 07:30, 17 March 2021
Line 1:		Line 1:

	==Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion==		==Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion==
-	<StructureSection load='2h2u' size='340' side='right' caption='[[2h2u]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='2h2u' size='340' side='right'caption='[[2h2u]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2h2u]] 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=2H2U OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2H2U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2h2u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H2U FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2h2n\|2h2n]], [[1s18\|1s18]], [[1s1d\|1s1d]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2h2n\|2h2n]], [[1s18\|1s18]], [[1s1d\|1s1d]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CANT1, SHAPY ([~~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">CANT1, SHAPY ([https://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/Nucleoside_diphosphate_phosphatase Nucleoside diphosphate phosphatase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nucleoside_diphosphate_phosphatase Nucleoside diphosphate phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [~~http~~://pdbe.org/2h2u PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2h2u PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2u 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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [https://pdbe.org/2h2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [https://www.ebi.ac.uk/pdbsum/2h2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2u ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN]] Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry.	+	[[https://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN]] Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN]] Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.<ref>PMID:12234496</ref> <ref>PMID:15248776</ref> <ref>PMID:22539336</ref>	+	[[https://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN]] Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.<ref>PMID:12234496</ref> <ref>PMID:15248776</ref> <ref>PMID:22539336</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h2u_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h2u_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 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Nucleoside diphosphate phosphatase]]		[[Category: Nucleoside diphosphate phosphatase]]
	[[Category: Herr, A B]]		[[Category: Herr, A B]]

OCA at 08:05, 18 October 2017

2017-10-18T08:05:34Z

←Older revision		Revision as of 08:05, 18 October 2017
Line 1:		Line 1:
		+
	==Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion==		==Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion==
	<StructureSection load='2h2u' size='340' side='right' caption='[[2h2u]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2h2u' size='340' side='right' caption='[[2h2u]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CANT1, SHAPY ([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">CANT1, SHAPY ([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/Nucleoside_diphosphate_phosphatase Nucleoside diphosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside_diphosphate_phosphatase Nucleoside diphosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [http://pdbe.org/2h2u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [http://www.ebi.ac.uk/pdbsum/2h2u 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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [http://pdbe.org/2h2u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [http://www.ebi.ac.uk/pdbsum/2h2u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2u ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 03:02, 10 February 2016

2016-02-10T03:02:56Z

←Older revision		Revision as of 03:02, 10 February 2016
Line 21:		Line 21:
	<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=2h2u ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 04:44, 11 September 2015

2015-09-11T04:44:41Z

←Older revision		Revision as of 04:44, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2h2u' size='340' side='right' caption='[[2h2u]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2h2u' size='340' side='right' caption='[[2h2u]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2h2u]] 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=2H2U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H2U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2h2u]] 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=2H2U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H2U FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2h2n\|2h2n]], [[1s18\|1s18]], [[1s1d\|1s1d]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2h2n\|2h2n]], [[1s18\|1s18]], [[1s1d\|1s1d]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CANT1, SHAPY ([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">CANT1, SHAPY ([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/Nucleoside~~-diphosphatase Nucleoside-diphosphatase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside_diphosphate_phosphatase Nucleoside diphosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [http://www.ebi.ac.uk/pdbsum/2h2u 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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [http://pdbe.org/2h2u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [http://www.ebi.ac.uk/pdbsum/2h2u PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 31:		Line 31:
	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 2h2u" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
-	[[Category: Nucleoside~~-diphosphatase~~]]	+	[[Category: Nucleoside diphosphate phosphatase]]
	[[Category: Herr, A B]]		[[Category: Herr, A B]]
	[[Category: Horii, K]]		[[Category: Horii, K]]

OCA at 08:16, 16 January 2015

2015-01-16T08:16:47Z

←Older revision		Revision as of 08:16, 16 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2h2u]] 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=2H2U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H2U FirstGlance]. <br>		<table><tr><td colspan='2'>[[2h2u]] 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=2H2U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H2U FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2h2n\|2h2n]], [[1s18\|1s18]], [[1s1d\|1s1d]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2h2n\|2h2n]], [[1s18\|1s18]], [[1s1d\|1s1d]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CANT1, SHAPY ([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">CANT1, SHAPY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphatase Nucleoside-diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphatase Nucleoside-diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [http://www.ebi.ac.uk/pdbsum/2h2u 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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [http://www.ebi.ac.uk/pdbsum/2h2u PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN]] Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry.		[[http://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN]] Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry.
Line 37:		Line 37:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Nucleoside-diphosphatase]]		[[Category: Nucleoside-diphosphatase]]
-	[[Category: Herr, A B.]]	+	[[Category: Herr, A B]]
-	[[Category: Horii, K.]]	+	[[Category: Horii, K]]
-	[[Category: Kirley, T L.]]	+	[[Category: Kirley, T L]]
-	[[Category: Yang, M.]]	+	[[Category: Yang, M]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Five-blade beta propeller]]		[[Category: Five-blade beta propeller]]

OCA: Protected "2h2u" [edit=sysop:move=sysop]

2014-09-30T07:57:28Z

Protected "2h2u" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:57, 30 September 2014

OCA at 07:57, 30 September 2014

2014-09-30T07:57:26Z

←Older revision		Revision as of 07:57, 30 September 2014
Line 1:		Line 1:
-	~~{{Seed}}~~	+	==Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion==
-	[[~~Image:~~2h2u.~~png~~\|~~left~~\|200px]]	+	<StructureSection load='2h2u' size='340' side='right' caption='[[2h2u]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2h2u]] 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=2H2U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H2U FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2h2n\|2h2n]], [[1s18\|1s18]], [[1s1d\|1s1d]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CANT1, SHAPY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphatase Nucleoside-diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </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=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [http://www.ebi.ac.uk/pdbsum/2h2u PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN]] Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN]] Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.<ref>PMID:12234496</ref> <ref>PMID:15248776</ref> <ref>PMID:22539336</ref>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h2u_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 ==
		+	Mammals express a protein homologous to soluble nucleotidases used by blood-sucking insects to inhibit host blood clotting. These vertebrate nucleotidases may play a role in protein glycosylation. The activity of this enzyme family is strictly dependent on calcium, which induces a conformational change in the secreted, soluble human nucleotidase. The crystal structure of this human enzyme was recently solved; however, the mechanism of calcium activation and the basis for the calcium-induced changes remain unclear. In this study, using analytical ultracentrifugation and chemical cross-linking, we show that calcium or strontium induce noncovalent dimerization of the soluble human enzyme. The location and nature of the dimer interface was elucidated using a combination of site-directed mutagenesis and chemical cross-linking, coupled with crystallographic analyses. Replacement of Ile(170), Ser(172), and Ser(226) with cysteine residues resulted in calcium-dependent, sulfhydryl-specific intermolecular cross-linking, which was not observed after cysteine introduction at other surface locations. Analysis of a super-active mutant, E130Y, revealed that this mutant dimerized more readily than the wild-type enzyme. The crystal structure of the E130Y mutant revealed that the mutated residue is found in the dimer interface. In addition, expression of the full-length nucleotidase revealed that this membrane-bound form can also dimerize and that these dimers are stabilized by spontaneous oxidative cross-linking of Cys(30), located between the single transmembrane helix and the start of the soluble sequence. Thus, calcium-mediated dimerization may also represent a mechanism for regulation of the activity of this nucleotidase in the physiological setting of the endoplasmic reticulum or Golgi.

-	<!--	+	Calcium-dependent dimerization of human soluble calcium activated nucleotidase: characterization of the dimer interface.,Yang M, Horii K, Herr AB, Kirley TL J Biol Chem. 2006 Sep 22;281(38):28307-17. Epub 2006 Jul 11. PMID:16835225<ref>PMID:16835225</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_2h2u"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display~~.	+
-	-->	+
-	~~{{STRUCTURE_2h2u\| PDB=2h2u \| SCENE= }}~~	+

-	~~===Crystal structure~~ of the ~~E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_16835225}}, adds the Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 16835225 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_16835225}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~2H2U is a 2 chains structure of sequences 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=2H2U OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:16835225<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Nucleoside-diphosphatase]]		[[Category: Nucleoside-diphosphatase]]
Line 32:		Line 43:
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Five-blade beta propeller]]		[[Category: Five-blade beta propeller]]
		+	[[Category: Hydrolase]]
	[[Category: Nucleotidase]]		[[Category: Nucleotidase]]
	[[Category: Nucleotide-binding]]		[[Category: Nucleotide-binding]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:54:27 2009''

OCA at 12:54, 17 February 2009

2009-02-17T12:54:28Z

←Older revision		Revision as of 12:54, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	2H2U is a ~~[[Single protein]]~~ structure of ~~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=2H2U OCA].	+	2H2U is a 2 chains structure of sequences 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=2H2U OCA].

	==Reference==		==Reference==
-	Calcium-dependent dimerization of human soluble calcium activated nucleotidase: characterization of the dimer interface., Yang M, Horii K, Herr AB, Kirley TL, J Biol Chem. 2006 Sep 22;281(38):28307-17. Epub 2006 Jul 11. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/16835225 16835225]~~	+	<ref group="xtra">PMID:16835225</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Nucleoside-diphosphatase]]		[[Category: Nucleoside-diphosphatase]]
-	[[Category: Single protein]]
	[[Category: Herr, A B.]]		[[Category: Herr, A B.]]
	[[Category: Horii, K.]]		[[Category: Horii, K.]]
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	[[Category: Nucleotide-binding]]		[[Category: Nucleotide-binding]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28 20~~:26:~~34 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:54:27 2009''

OCA at 17:26, 28 July 2008

2008-07-28T17:26:37Z

←Older revision		Revision as of 17:26, 28 July 2008
Line 1:		Line 1:
-	[[Image:2h2u.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:2h2u.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_2h2u\| PDB=2h2u \| SCENE= }}		{{STRUCTURE_2h2u\| PDB=2h2u \| SCENE= }}

-	~~'''~~Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion~~'''~~	+	===Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion===


-	~~==Overview==~~	+	<!--
-	~~Mammals express a protein homologous to soluble nucleotidases used by blood-sucking insects to inhibit host blood clotting. These vertebrate nucleotidases may play a role in protein glycosylation.~~ The ~~activity of~~ this ~~enzyme family is strictly dependent on calcium~~, ~~which induces a conformational change in the secreted, soluble human nucleotidase. The crystal structure of this human enzyme was recently solved; however~~, the ~~mechanism of calcium activation and~~ the ~~basis for the calcium-induced changes remain unclear~~. ~~In this study, using analytical ultracentrifugation and chemical cross-linking, we show that calcium or strontium induce noncovalent dimerization of the soluble human enzyme~~. The location and nature of the dimer interface was elucidated using a combination of site-directed mutagenesis and chemical cross-linking, coupled with crystallographic analyses. Replacement of Ile(170), Ser(172), and Ser(226) with cysteine residues resulted in calcium-dependent, sulfhydryl-specific intermolecular cross-linking, which was not observed after cysteine introduction at other surface locations. Analysis of a super-active mutant, E130Y, revealed that this mutant dimerized more readily than the wild-type enzyme. The crystal structure of the E130Y mutant revealed that the mutated residue is ~~found in~~ the ~~dimer interface~~. ~~In addition, expression of the full~~-~~length nucleotidase revealed that this membrane~~-bound form can also dimerize and that these dimers are stabilized by spontaneous oxidative cross-linking of Cys(30), located between the single transmembrane helix and the start of the soluble sequence. Thus, calcium-mediated dimerization may also represent a mechanism for regulation of the activity of this nucleotidase in the physiological setting of the endoplasmic reticulum or Golgi.	+	The line below this paragraph, {{ABSTRACT_PUBMED_16835225}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 16835225 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_16835225}}

	==About this Structure==		==About this Structure==
Line 31:		Line 35:
	[[Category: Nucleotidase]]		[[Category: Nucleotidase]]
	[[Category: Nucleotide-binding]]		[[Category: Nucleotide-binding]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 05~~:48:11 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:26:34 2008''