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The bacterial Sec-translocase: structure and mechanism.

ABSTRACT: 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.

SUBMITTER: Lycklama A Nijeholt JA

PROVIDER: S-EPMC3297432 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature

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The bacterial Sec-translocase: structure and mechanism.

Lycklama A Nijeholt Jelger A JA Driessen Arnold J M AJ

Philosophical transactions of the Royal Society of London. Series B, Biological sciences 20120401 1592

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. ...[more]

PMID: 22411975

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