2p32
From Proteopedia
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Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70
Overview
Hsp70 chaperones are composed of two domains; the 40kDa N-terminal, nucleotide-binding domain (NDB) and the 30kDa 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 18kDa beta-sandwich, subdomain, which forms the hydrophobic binding pocket, and a 10kDa, 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 10kDa 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 with as ligand. 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 Mar 28;. PMID:17407764
Page seeded by OCA on Wed Jan 23 15:19:51 2008
