SecB--a chaperone dedicated to protein translocation.
SecB is a molecular chaperone in Gram-negative bacteria dedicated to the post-translational translocation of proteins across the cytoplasmic membrane. The entire surface of this chaperone is used for both of its native functions in protein targeting and unfolding. Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation.
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands. a.j.m.driessen@rug.nl.
Philipp
P
Bechtluft
Nico
N
Nouwen
Sander J
SJ
Tans
Arnold J M
AJ
Driessen
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D006090:Gram-Negative Bacteria / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D021381:Protein Transport; D049490:Systems Biology
D001426:Bacterial Proteins; D018832:Molecular Chaperones; C057842:SecB protein, Bacteria