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
SN - 0962-8436
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
IS - 1592
ER -