PMID: 11336818May 5, 2001Paper

SecB, a molecular chaperone with two faces

Trends in Microbiology
A J Driessen

Abstract

SecB is a molecular chaperone unique to the phylum Proteobacteria, which includes the majority of known Gram-negative bacteria of medical, industrial and agricultural significance. SecB is involved in the translocation of secretory proteins across the cytoplasmic membrane. The crystal structure of the Haemophilus influenzae SecB provides new insights into how SecB simultaneously recognizes its two ligands: unfolded preproteins and SecA, the ATPase subunit of the translocase. SecB uses its entire molecular surface for these two functions, but for preprotein release and its own membrane release, SecB relies on the catalytic activity of SecA. This defines SecB as a translocation-specific molecular chaperone.

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Citations

Dec 20, 2002·Angewandte Chemie·Stefan Walter, Johannes Buchner
Mar 7, 2003·FEMS Microbiology Letters·Mario F Feldman, Guy R Cornelis
Oct 13, 2001·Trends in Microbiology·H Mori, K Ito
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Oct 26, 2010·The Journal of Biological Chemistry·Patrick J BakkesLutz Schmitt
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