2p32

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[[Image:2p32.gif|left|200px]]
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{{Structure
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|GENE= hsp-1, hsp70a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])
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{{STRUCTURE_2p32| PDB=2p32 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p32 OCA], [http://www.ebi.ac.uk/pdbsum/2p32 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2p32 RCSB]</span>
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'''Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70'''
'''Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70'''
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[[Category: Walkinshaw, M D.]]
[[Category: Walkinshaw, M D.]]
[[Category: Worrall, L J.]]
[[Category: Worrall, L J.]]
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[[Category: three-helix bundle]]
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[[Category: Three-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:14:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:28:05 2008''
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Revision as of 09:14, 4 May 2008

Template:STRUCTURE 2p32

Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70


Overview

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.

About this Structure

2P32 is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 12:14:15 2008

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