2p32

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17407764 17407764]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17407764 17407764]
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Walkinshaw, M.D.]]
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[[Category: Walkinshaw, M D.]]
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[[Category: Worrall, L.J.]]
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[[Category: Worrall, L J.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: three-helix bundle]]
[[Category: three-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:19:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:25:20 2008''

Revision as of 16:25, 21 February 2008


2p32, resolution 3.200Å

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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 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 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 May 25;357(1):105-10. Epub 2007 Mar 28. PMID:17407764

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