2B26

The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1

2B26 の概要

• エントリーDOI: 10.2210/pdb2b26/pdb
• 分子名称: SIS1 protein, Heat shock 70 kDa protein cognate 2 (2 entities in total)
• 機能のキーワード: hsp40 sis1 hsp70 ssa1, chaperone-protein transport complex, chaperone/protein transport
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 59252.38

構造登録者

Li, J.,Wu, Y.,Qian, X.,Sha, B. (登録日: 2005-09-16, 公開日: 2006-09-19, 最終更新日: 2024-02-14)

主引用文献

Li, J.,Wu, Y.,Qian, X.,Sha, B.
Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex.
Biochem.J., 398:353-360, 2006

PubMed Abstract: Heat shock protein (Hsp) 40 facilitates the critical role of Hsp70 in a number of cellular processes such as protein folding, assembly, degradation and translocation in vivo. Hsp40 and Hsp70 stay in close contact to achieve these diverse functions. The conserved C-terminal EEVD motif in Hsp70 has been shown to regulate Hsp40-Hsp70 interaction by an unknown mechanism. Here, we provide a structural basis for this regulation by determining the crystal structure of yeast Hsp40 Sis1 peptide-binding fragment complexed with the Hsp70 Ssa1 C-terminal. The Ssa1 extreme C-terminal eight residues, G634PTVEEVD641, form a beta-strand with the domain I of Sis1 peptide-binding fragment. Surprisingly, the Ssa1 C-terminal binds Sis1 at the site where Sis1 interacts with the non-native polypeptides. The negatively charged residues within the EEVD motif in Ssa1 C-terminal form extensive charge-charge interactions with the positively charged residues in Sis1. The structure-based mutagenesis data support the structural observations.

PubMed: 16737444
DOI: 10.1042/BJ20060618

実験手法

X-RAY DIFFRACTION (3.2 Å)