3d2e - Revision history

OCA at 08:56, 30 October 2024

2024-10-30T08:56:43Z

← Older revision		Revision as of 08:56, 30 October 2024
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	<StructureSection load='3d2e' size='340' side='right'caption='[[3d2e]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='3d2e' size='340' side='right'caption='[[3d2e]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3d2e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_18824 Atcc 18824~~] and [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D2E FirstGlance]. <br>		<table><tr><td colspan='2'>[[3d2e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D2E FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ATP:ADENOSINE-5~~-~~TRIPHOSPHATE'>ATP</scene>~~, ~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.35Å</td></tr>
	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~MSE~~:~~SELENOMETHIONINE~~'>~~MSE~~</scene><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td><~~td class~~=~~"sblockDat"><div style~~=~~'overflow~~: ~~auto; max-height: 3em;~~'>~~[[3d2f\|3d2f]]~~</~~div~~><~~/td></tr>~~
	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></~~td><td class="sblockDat"~~>SSE1, MSI3, YPL106C, LPG3C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), HSPA1A, HSPA1, HSPA1B ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3d2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2e OCA], [https://pdbe.org/3d2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d2e RCSB], [https://www.ebi.ac.uk/pdbsum/3d2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d2e 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=3d2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2e OCA], [https://pdbe.org/3d2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d2e RCSB], [https://www.ebi.ac.uk/pdbsum/3d2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d2e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/HSP7F_YEAST HSP7F_YEAST]] Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.		[https://www.uniprot.org/uniprot/HSP7F_YEAST HSP7F_YEAST] Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d2/3d2e_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d2/3d2e_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Atcc 18824]]~~		[[Category: Homo sapiens]]
	~~[[Category: Human~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Bracher, A~~]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: ~~Polier, S~~]]		[[Category: Bracher A]]
	[[Category: ~~Atp-binding]]~~		[[Category: Polier S]]
	~~[[Category: Calmodulin-binding]]~~
	~~[[Category: Chaperone]]~~
	~~[[Category: Nucleotide exchange factor]]~~
	~~[[Category: Nucleotide-binding]]~~
	~~[[Category: Phosphoprotein]]~~
	~~[[Category: Protein folding]]~~
	~~[[Category: Stress response~~]]

OCA at 07:51, 2 February 2022

2022-02-02T07:51:26Z

← Older revision		Revision as of 07:51, 2 February 2022
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	==Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals==		==Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals==
	<StructureSection load='3d2e' size='340' side='right' caption='[[3d2e]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='3d2e' size='340' side='right'caption='[[3d2e]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3d2e]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3D2E FirstGlance]. <br>		<table><tr><td colspan='2'>[[3d2e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D2E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d2f\|3d2f]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3d2f\|3d2f]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SSE1, MSI3, YPL106C, LPG3C ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), HSPA1A, HSPA1, HSPA1B ([~~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">SSE1, MSI3, YPL106C, LPG3C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), HSPA1A, HSPA1, HSPA1B ([https://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=3d2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2e OCA], [~~http~~://pdbe.org/3d2e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3d2e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3d2e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3d2e 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=3d2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2e OCA], [https://pdbe.org/3d2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d2e RCSB], [https://www.ebi.ac.uk/pdbsum/3d2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d2e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/HSP7F_YEAST HSP7F_YEAST]] Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.		[[https://www.uniprot.org/uniprot/HSP7F_YEAST HSP7F_YEAST]] Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.
	== 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/d2/3d2e_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d2/3d2e_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 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 3d2e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3d2e" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Atcc 18824]]		[[Category: Atcc 18824]]
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Bracher, A]]		[[Category: Bracher, A]]
	[[Category: Polier, S]]		[[Category: Polier, S]]

OCA at 05:07, 16 November 2017

2017-11-16T05:07:32Z

← Older revision		Revision as of 05:07, 16 November 2017
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	</div>		</div>
	<div class="pdbe-citations 3d2e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3d2e" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Heat Shock Proteins\|Heat Shock Proteins]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 00:48, 5 August 2016

2016-08-05T00:48:27Z

← Older revision		Revision as of 00:48, 5 August 2016
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	==Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals==		==Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals==
	<StructureSection load='3d2e' size='340' side='right' caption='[[3d2e]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='3d2e' size='340' side='right' caption='[[3d2e]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3d2e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~] and [http://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae Saccharomyces cerevisiae~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D2E FirstGlance]. <br>		<table><tr><td colspan='2'>[[3d2e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D2E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d2f\|3d2f]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d2f\|3d2f]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SSE1, MSI3, YPL106C, LPG3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ~~Saccharomyces cerevisiae~~]), HSPA1A, HSPA1, HSPA1B ([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">SSE1, MSI3, YPL106C, LPG3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), HSPA1A, HSPA1, HSPA1B ([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=3d2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d2e RCSB], [http://www.ebi.ac.uk/pdbsum/3d2e 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=3d2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2e OCA], [http://pdbe.org/3d2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d2e RCSB], [http://www.ebi.ac.uk/pdbsum/3d2e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3d2e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	<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=3d2e ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	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 3d2e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Atcc 18824]]
	[[Category: ~~Saccharomyces cerevisiae~~]]		[[Category: Human]]
	[[Category: Bracher, A]]		[[Category: Bracher, A]]
	[[Category: Polier, S]]		[[Category: Polier, S]]

OCA at 14:29, 25 December 2014

2014-12-25T14:29:25Z

← Older revision		Revision as of 14:29, 25 December 2014
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	<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=3d2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d2e RCSB], [http://www.ebi.ac.uk/pdbsum/3d2e 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=3d2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d2e RCSB], [http://www.ebi.ac.uk/pdbsum/3d2e PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/HSP7F_YEAST HSP7F_YEAST]] Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 14:09, 18 December 2014

2014-12-18T14:09:19Z

← Older revision		Revision as of 14:09, 18 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_3d2e\| PDB=3d2e \| SCENE= }}~~		==Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals==
	===Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals===		<StructureSection load='3d2e' size='340' side='right' caption='[[3d2e]], [[Resolution\|resolution]] 2.35Å' scene=''>
	~~{{ABSTRACT_PUBMED_18555782}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3d2e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D2E FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
			<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d2f\|3d2f]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SSE1, MSI3, YPL106C, LPG3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), HSPA1A, HSPA1, HSPA1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3d2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d2e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d2e RCSB], [http://www.ebi.ac.uk/pdbsum/3d2e PDBsum]</span></td></tr>
			</table>
			== 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/d2/3d2e_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 ==
			Protein folding by Hsp70 is tightly controlled by cochaperones, including J-domain proteins that trigger ATP hydrolysis and nucleotide exchange factors (NEFs) that remove ADP from Hsp70. Here we present the crystal structure of the yeast NEF Sse1p (Hsp110) in complex with the nucleotide-binding domain (NBD) of Hsp70. Hsp110 proteins are homologous to Hsp70s and consist of an NBD, a beta sandwich domain, and a three helix bundle domain (3HBD). In the complex, the NBD of Sse1p is ATP bound, and together with the 3HBD it embraces the NBD of Hsp70, inducing opening and the release of bound ADP from Hsp70. Mutations that abolish NEF activity are lethal, thus defining nucleotide exchange on Hsp70 as an essential function of Sse1p. Our data suggest that Sse1p does not employ the nucleotide-dependent allostery and peptide-binding mode of canonical Hsp70s, and that direct interactions of substrate with Sse1p may support Hsp70-assisted protein folding in a cooperative process.

	~~==Function==~~		Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.,Polier S, Dragovic Z, Hartl FU, Bracher A Cell. 2008 Jun 13;133(6):1068-79. PMID:18555782<ref>PMID:18555782</ref>
	~~[[http://www~~.~~uniprot~~.~~org/uniprot/HSP7F_YEAST HSP7F_YEAST]] Has a calcium~~-~~dependent calmodulin-binding activity. Required for normal growth at various temperatures~~.

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[3d2e]] is~~ a ~~4 chain structure with sequence from [http://en.wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens] and [http://en~~.~~wikipedia~~.~~org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il~~/~~oca-bin/ocashort?id=3D2E OCA].~~		</div>

	==~~Reference~~==		==See Also==
	~~<ref group~~=~~"xtra">PMID:018555782</ref>~~<references ~~group="xtra"~~/><~~references~~/>		*[[Heat Shock Proteins\|Heat Shock Proteins]]
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Bracher, A.]]		[[Category: Bracher, A]]
	[[Category: Polier, S.]]		[[Category: Polier, S]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]
	[[Category: Calmodulin-binding]]		[[Category: Calmodulin-binding]]

OCA at 09:00, 19 June 2013

2013-06-19T09:00:44Z

← Older revision		Revision as of 09:00, 19 June 2013
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	~~[[Image:3d2e.png\|left\|200px]]~~

	{{STRUCTURE_3d2e\| PDB=3d2e \| SCENE= }}		{{STRUCTURE_3d2e\| PDB=3d2e \| SCENE= }}

	===Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals===		===Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals===
			{{ABSTRACT_PUBMED_18555782}}

	~~{{ABSTRACT_PUBMED_018555782}}~~		==Function==
			[[http://www.uniprot.org/uniprot/HSP7F_YEAST HSP7F_YEAST]] Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.

	==About this Structure==		==About this Structure==
	[[3d2e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA].		[[3d2e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA].

	~~==See Also==~~
	*[[Heat Shock Proteins\|Heat Shock Proteins]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:018555782</ref><references group="xtra"/>		<ref group="xtra">PMID:018555782</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]

OCA at 17:50, 20 October 2012

2012-10-20T17:50:05Z

← Older revision		Revision as of 17:50, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[3d2e]] is a 4 chain structure ~~of [[Heat Shock Proteins]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA].		[[3d2e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA].

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

OCA: Protected "3d2e" [edit=sysop:move=sysop]

2012-07-27T02:08:54Z

Protected "3d2e" [edit=sysop:move=sysop]

← Older revision	Revision as of 02:08, 27 July 2012
(No difference)

OCA at 02:08, 27 July 2012

2012-07-27T02:08:53Z

← Older revision		Revision as of 02:08, 27 July 2012
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	~~{{Seed}}~~
	[[Image:3d2e.png\|left\|200px]]		[[Image:3d2e.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3d2e", 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_3d2e\| PDB=3d2e \| SCENE= }}		{{STRUCTURE_3d2e\| PDB=3d2e \| SCENE= }}

	===Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals===		===Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals===

			{{ABSTRACT_PUBMED_018555782}}

	==About this Structure==		==About this Structure==
	~~3D2E~~ is a 4 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA].		[[3d2e]] is a 4 chain structure of [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D2E OCA].

			==See Also==
			*[[Heat Shock Proteins\|Heat Shock Proteins]]

			==Reference==
			<ref group="xtra">PMID:018555782</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Bracher, A.]]		[[Category: Bracher, A.]]
	[[Category: Polier, S.]]		[[Category: Polier, S.]]
	~~[[Category: Acetylation]]~~
	[[Category: Atp-binding]]		[[Category: Atp-binding]]
	[[Category: Calmodulin-binding]]		[[Category: Calmodulin-binding]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
	~~[[Category: Cytoplasm]]~~
	[[Category: Nucleotide exchange factor]]		[[Category: Nucleotide exchange factor]]
	[[Category: Nucleotide-binding]]		[[Category: Nucleotide-binding]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
	~~[[Category: Polymorphism]]~~
	[[Category: Protein folding]]		[[Category: Protein folding]]
	[[Category: Stress response]]		[[Category: Stress response]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:43:36 2009''~~