3i33

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==Crystal structure of the human 70kDa heat shock protein 2 (Hsp70-2) ATPase domain in complex with ADP and inorganic phosphate==
==Crystal structure of the human 70kDa heat shock protein 2 (Hsp70-2) ATPase domain in complex with ADP and inorganic phosphate==
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<StructureSection load='3i33' size='340' side='right' caption='[[3i33]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<StructureSection load='3i33' size='340' side='right'caption='[[3i33]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3i33]] is a 1 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=3I33 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I33 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3i33]] is a 1 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=3I33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I33 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fe1|3fe1]], [[3gdq|3gdq]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i33 OCA], [https://pdbe.org/3i33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i33 RCSB], [https://www.ebi.ac.uk/pdbsum/3i33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i33 ProSAT]</span></td></tr>
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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=3i33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i33 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i33 RCSB], [http://www.ebi.ac.uk/pdbsum/3i33 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HSP72_HUMAN HSP72_HUMAN]] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage.
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[https://www.uniprot.org/uniprot/HSP72_HUMAN HSP72_HUMAN] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i3/3i33_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i3/3i33_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>
</jmolCheckbox>
</jmolCheckbox>
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</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].
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</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=3i33 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3i33" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Heat Shock Proteins|Heat Shock Proteins]]
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H]]
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[[Category: Large Structures]]
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[[Category: Berg, S Van den]]
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[[Category: Arrowsmith CH]]
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[[Category: Berglund, H]]
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[[Category: Berglund H]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Collins, R]]
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[[Category: Collins R]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Flodin, S]]
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[[Category: Flodin S]]
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[[Category: Flores, A]]
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[[Category: Flores A]]
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[[Category: Graslund, S]]
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[[Category: Graslund S]]
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[[Category: Hammarstrom, M]]
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[[Category: Hammarstrom M]]
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[[Category: Johansson, A]]
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[[Category: Johansson A]]
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[[Category: Johansson, I]]
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[[Category: Johansson I]]
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[[Category: Karlberg, T]]
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[[Category: Karlberg T]]
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[[Category: Kotenyova, T]]
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[[Category: Kotenyova T]]
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[[Category: Kotzsch, A]]
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[[Category: Kotzsch A]]
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[[Category: Moche, M]]
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[[Category: Moche M]]
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[[Category: Nielsen, T K]]
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[[Category: Nielsen TK]]
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[[Category: Nordlund, P]]
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[[Category: Nordlund P]]
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[[Category: Nyman, T]]
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[[Category: Nyman T]]
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[[Category: Persson, C]]
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[[Category: Persson C]]
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[[Category: Roos, A K]]
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[[Category: Roos AK]]
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[[Category: Structural genomic]]
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[[Category: Sagemark J]]
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[[Category: Sagemark, J]]
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[[Category: Schueler H]]
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[[Category: Schueler, H]]
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[[Category: Schutz P]]
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[[Category: Schutz, P]]
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[[Category: Siponen MI]]
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[[Category: Siponen, M I]]
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[[Category: Thorsell AG]]
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[[Category: Thorsell, A G]]
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[[Category: Tresaugues L]]
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[[Category: Tresaugues, L]]
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[[Category: Van den Berg S]]
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[[Category: Weigelt, J]]
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[[Category: Weigelt J]]
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[[Category: Welin, M]]
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[[Category: Welin M]]
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[[Category: Wisniewska, M]]
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[[Category: Wisniewska M]]
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[[Category: Atp-binding]]
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[[Category: Chaperone]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Protein-adp complex]]
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[[Category: Sgc]]
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[[Category: Stress response]]
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Current revision

Crystal structure of the human 70kDa heat shock protein 2 (Hsp70-2) ATPase domain in complex with ADP and inorganic phosphate

PDB ID 3i33

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OCA

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