2p32
From Proteopedia
(Difference between revisions)
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<StructureSection load='2p32' size='340' side='right'caption='[[2p32]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='2p32' size='340' side='right'caption='[[2p32]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2p32]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2p32]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P32 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p32 OCA], [https://pdbe.org/2p32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p32 RCSB], [https://www.ebi.ac.uk/pdbsum/2p32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p32 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=2p32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p32 OCA], [https://pdbe.org/2p32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p32 RCSB], [https://www.ebi.ac.uk/pdbsum/2p32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p32 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HSP1_CAEEL HSP1_CAEEL] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=2p32 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=2p32 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Hsp70 chaperones are composed of two domains; the 40 kDa N-terminal nucleotide-binding domain (NDB) and the 30 kDa C-terminal substrate-binding domain (SBD). Structures of the SBD from Escherichia coli homologues DnaK and HscA show it can be further divided into an 18 kDa beta-sandwich subdomain, which forms the hydrophobic binding pocket, and a 10 kDa C-terminal three-helix bundle that forms a lid over the binding pocket. Across prokaryotes and eukaryotes, the NBD and beta-sandwich subdomain are well conserved in both sequence and structure. The C-terminal subdomain is, however, more evolutionary variable and the only eukaryotic structure from rat Hsc70 revealed a diverged helix-loop-helix fold. We have solved the crystal structure of the C-terminal 10 kDa subdomain from Caenorhabditis elegans Hsp70 which forms a helical-bundle similar to the prokaryotic homologues. This provides the first confirmation of the structural conservation of this subdomain in eukaryotes. Comparison with the rat structure reveals a domain-swap dimerisation mechanism; however, the C. elegans subdomain exists exclusively as a monomer in solution in agreement with the hypothesis that regions out with the C-terminal subdomain are necessary for Hsp70 self-association. | ||
| - | |||
| - | Crystal structure of the C-terminal three-helix bundle subdomain of C. elegans Hsp70.,Worrall LJ, Walkinshaw MD Biochem Biophys Res Commun. 2007 May 25;357(1):105-10. Epub 2007 Mar 28. PMID:17407764<ref>PMID:17407764</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2p32" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Caenorhabditis elegans]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Walkinshaw | + | [[Category: Walkinshaw MD]] |
| - | [[Category: Worrall | + | [[Category: Worrall LJ]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70
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