Crystal structure of SecB from Escherichia coli

被引:53
作者
Dekker, C
de Kruijff, B
Gros, P
机构
[1] Natl Inst Med Res, London NW7 1AA, England
[2] Univ Utrecht, Dept Crystal & Struct Chem, NL-3584 CH Utrecht, Netherlands
[3] Univ Utrecht, Dept Biochem Membranes, NL-3584 CH Utrecht, Netherlands
关键词
SecB; chaperone; crystal structure; protein translocation; Escherichia coli;
D O I
10.1016/j.jsb.2003.09.012
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The chaperone SecB from Escherichia coli is primarily involved in passing precursor proteins into the See system via specific interactions with SecA. The crystal structure of SecB from E coli has been solved to 2.35 Angstrom resolution. The structure shows flexibility in the crossover loop and the helix-connecting loop, regions that have been implicated to be part of the SecB substrate-binding site. Moreover conformational variability of Trp36 is observed as well as different loop conformations for the different monomers. Based on this, we speculate that SecB can regulate the access or extent of its hydrophobic substrate-binding site, by modulating the conformation of the crossover loop and the helix-connecting loop. The structure also clearly explains why the tetrameric equilibrium is shifted towards the dimeric state in the mutant SecBCys76Tyr. The buried cysteine residue is crucial for tight packing, and mutations are likely to disrupt the tetramer formation but not the dimer formation. (C) 2003 Elsevier Inc. All rights reserved.
引用
收藏
页码:313 / 319
页数:7
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