2P32

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

2P32 の概要

• エントリーDOI: 10.2210/pdb2p32/pdb
• 分子名称: Heat shock 70 kDa protein A, SULFATE ION (2 entities in total)
• 機能のキーワード: three-helix bundle, chaperone
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 78320.14

構造登録者

Worrall, L.J.,Walkinshaw, M.D. (登録日: 2007-03-08, 公開日: 2007-04-17, 最終更新日: 2024-04-03)

主引用文献

Worrall, L.J.,Walkinshaw, M.D.
Crystal structure of the C-terminal three-helix bundle subdomain of C. elegans Hsp70.
Biochem.Biophys.Res.Commun., 357:105-110, 2007

PubMed Abstract: 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.

PubMed: 17407764
DOI: 10.1016/j.bbrc.2007.03.107

実験手法

X-RAY DIFFRACTION (3.2 Å)