1VZY

Crystal structure of the Bacillus subtilis HSP33

1VZY の概要

• エントリーDOI: 10.2210/pdb1vzy/pdb
• 分子名称: 33 KDA CHAPERONIN, ZINC ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: chaperone, heat shock protein, crystal engineering, molecular chaperone, redox-active center, psi, protein structure initiative, mcsg, midwest center for structural genomics
• 由来する生物種: Bacillus subtilis 168
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63947.25

構造登録者

Janda, I.K.,Devedjiev, Y.,Derewenda, U.,Dauter, Z.,Bielnicki, J.,Cooper, D.R.,Joachimiak, A.,Derewenda, Z.S.,Midwest Center for Structural Genomics (MCSG) (登録日: 2004-05-29, 公開日: 2004-10-06, 最終更新日: 2024-05-08)

主引用文献

Janda, I.,Devedjiev, Y.,Derewenda, U.,Dauter, Z.,Bielnicki, J.,Cooper, D.R.,Graf, P.C.,Joachimiak, A.,Jakob, U.,Derewenda, Z.S.
The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism.
Structure, 12:1901-1907, 2004

PubMed Abstract: The bacterial heat shock protein Hsp33 is a redox-regulated chaperone activated by oxidative stress. In response to oxidation, four cysteines within a Zn2+ binding C-terminal domain form two disulfide bonds with concomitant release of the metal. This leads to the formation of the biologically active Hsp33 dimer. The crystal structure of the N-terminal domain of the E. coli protein has been reported, but neither the structure of the Zn2+ binding motif nor the nature of its regulatory interaction with the rest of the protein are known. Here we report the crystal structure of the full-length B. subtilis Hsp33 in the reduced form. The structure of the N-terminal, dimerization domain is similar to that of the E. coli protein, although there is no domain swapping. The Zn2+ binding domain is clearly resolved showing the details of the tetrahedral coordination of Zn2+ by four thiolates. We propose a structure-based activation pathway for Hsp33.

PubMed: 15458638
DOI: 10.1016/j.str.2004.08.003

実験手法

X-RAY DIFFRACTION (1.97 Å)