Conformational plasticity of molecular chaperones involved in periplasmic and outer membrane protein folding
Author:
Affiliation:
1. Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland
Funder
Swiss National Science Foundation
Publisher
Oxford University Press (OUP)
Subject
Genetics,Molecular Biology,Microbiology
Link
http://academic.oup.com/femsle/article-pdf/365/13/fny121/25030193/fny121.pdf
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3. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity;Behrens;EMBO J,2001
4. The structure of a BamA-BamD fusion illuminates the architecture of the β-barrel assembly machine core;Bergal;Structure,2016
5. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins;Bitto;Structure,2002
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