Publication

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.

Research output: Contribution to journalReview articleAcademicpeer-review

APA

Lycklama a Nijeholt, J. A., & Driessen, A. J. M. (2012). The bacterial Sec-translocase: structure and mechanism. Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 367(1592), 1016-1028. https://doi.org/10.1098/rstb.2011.0201

Author

Lycklama a Nijeholt, Jelger A. ; Driessen, Arnold J. M. / The bacterial Sec-translocase : structure and mechanism. In: Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 2012 ; Vol. 367, No. 1592. pp. 1016-1028.

Harvard

Lycklama a Nijeholt, JA & Driessen, AJM 2012, 'The bacterial Sec-translocase: structure and mechanism', Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, vol. 367, no. 1592, pp. 1016-1028. https://doi.org/10.1098/rstb.2011.0201

Standard

The bacterial Sec-translocase : structure and mechanism. / Lycklama a Nijeholt, Jelger A.; Driessen, Arnold J. M.

In: Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, Vol. 367, No. 1592, 19.04.2012, p. 1016-1028.

Research output: Contribution to journalReview articleAcademicpeer-review

Vancouver

Lycklama a Nijeholt JA, Driessen AJM. The bacterial Sec-translocase: structure and mechanism. Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 2012 Apr 19;367(1592):1016-1028. https://doi.org/10.1098/rstb.2011.0201


BibTeX

@article{2fffac73b99e476ba10f83309b9f4898,
title = "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.",
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",
author = "{Lycklama a Nijeholt}, {Jelger A.} and Driessen, {Arnold J. M.}",
year = "2012",
month = apr,
day = "19",
doi = "10.1098/rstb.2011.0201",
language = "English",
volume = "367",
pages = "1016--1028",
journal = "Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences",
issn = "0962-8436",
publisher = "ROYAL SOC",
number = "1592",

}

RIS

TY - JOUR

T1 - The bacterial Sec-translocase

T2 - structure and mechanism

AU - Lycklama a Nijeholt, Jelger A.

AU - Driessen, Arnold J. M.

PY - 2012/4/19

Y1 - 2012/4/19

N2 - 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.

AB - 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.

KW - protein translocation

KW - membrane protein insertion

KW - SecY

KW - translocon

KW - SecA

KW - SIGNAL-SEQUENCE RECOGNITION

KW - PRECURSOR PROTEIN TRANSLOCATION

KW - ESCHERICHIA-COLI TRANSLOCASE

KW - LARGE CONFORMATIONAL-CHANGE

KW - BACILLUS-SUBTILIS SECA

KW - ATP-BINDING-SITE

KW - X-RAY-STRUCTURE

KW - PLUG DOMAIN

KW - PREPROTEIN TRANSLOCASE

KW - ENDOPLASMIC-RETICULUM

U2 - 10.1098/rstb.2011.0201

DO - 10.1098/rstb.2011.0201

M3 - Review article

VL - 367

SP - 1016

EP - 1028

JO - Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences

JF - Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences

SN - 0962-8436

IS - 1592

ER -

ID: 5520747