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The bacterial Sec-translocase: structure and mechanism

Lycklama a Nijeholt, J. A. & Driessen, A. J. M., 19-Apr-2012, In : Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 367, 1592, p. 1016-1028 13 p.

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  • The bacterial Sec-translocase structure and mechanism

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DOI

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.

Original languageEnglish
Pages (from-to)1016-1028
Number of pages13
JournalPhilosophical Transactions of the Royal Society of London. Series B: Biological Sciences
Volume367
Issue number1592
Publication statusPublished - 19-Apr-2012

    Keywords

  • 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

ID: 5520747