The bacterial Sec-translocase: structure and mechanism

被引：113
作者：
Nijeholt, Jelger A. Lycklama A.
Driessen, Arnold J. M. [1 ]
机构：
[1] Univ Groningen, Dept Mol Microbiol, Groningen Biomol Sci & Biotechnol Inst, NL-9747 AG Groningen, Netherlands
来源：
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES | 2012年 / 367卷 / 1592期
关键词：
protein translocation; membrane protein insertion; SecY; translocon; SecA; SIGNAL-SEQUENCE RECOGNITION; PRECURSOR PROTEIN TRANSLOCATION; ESCHERICHIA-COLI TRANSLOCASE; LARGE CONFORMATIONAL-CHANGE; BACILLUS-SUBTILIS SECA; ATP-BINDING-SITE; X-RAY-STRUCTURE; PLUG DOMAIN; PREPROTEIN TRANSLOCASE; ENDOPLASMIC-RETICULUM;
D O I：
10.1098/rstb.2011.0201
中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Most bacterial secretory proteins pass across the cytoplasmic membrane via the translocase, which consists of a protein-conducting channel SecYEG and an ATP-dependent motor protein SecA. The ancillary SecDF membrane protein complex promotes the final stages of translocation. Recent years have seen a major advance in our understanding of the structural and biochemical basis of protein translocation, and this has led to a detailed model of the translocation mechanism.
引用
收藏
页码：1016 / 1028
页数：13
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