Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients
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چکیده
منابع مشابه
The Activity and Specificity of the Outer Membrane Protein Chaperone SurA Are Modulated by a Proline Isomerase Domain
UNLABELLED SurA is a component of the periplasmic chaperone network that plays a central role in biogenesis of integral outer membrane β-barrel proteins (OMPs) in Escherichia coli. Although SurA contains two well-conserved proline isomerase (PPIase) domains, the contribution of these domains to SurA function is unclear. In the present work, we show that defects in OMP assembly caused by mutatio...
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متن کاملCrystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins.
The SurA protein facilitates correct folding of outer membrane proteins in gram-negative bacteria. The sequence of Escherichia coli SurA presents four segments, two of which are peptidyl-prolyl isomerases (PPIases); the crystal structure reveals an asymmetric dumbbell, in which the amino-terminal, carboxy-terminal, and first PPIase segments of the sequence form a core structural module, and the...
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ژورنال
عنوان ژورنال: Nature Communications
سال: 2020
ISSN: 2041-1723
DOI: 10.1038/s41467-020-15702-1