Crystal structure of the bacterial protein export chaperone SecB

被引:92
作者
Xu, ZH [1 ]
Knafels, JD [1 ]
Yoshino, K [1 ]
机构
[1] Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1038/82040
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
SecB is a bacterial molecular chaperone involved in mediating translocation of newly synthesized polypeptides across the cytoplasmic membrane of bacteria. The crystal structure of SecB from Haemophilus influenzae shows that the molecule is a tetramer organized as a dimer of dimers. Two long channels run along the side of the molecule. These are bounded by flexible loops and lined with conserved hydrophobic amino acids, which define a suitable environment for binding non-native polypeptides. The structure also reveals an acidic region on the top surface of the molecule, several residues of which have been implicated in binding to SecA, its downstream target.
引用
收藏
页码:1172 / 1177
页数:6
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