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Oxidation state-dependent protein-protein interactions in disulfide cascades.

Abstract:

Bacterial growth and pathogenicity depend on the correct formation of disulfide bonds, a process controlled by the Dsb system in the periplasm of Gram-negative bacteria. Proteins with a thioredoxin fold play a central role in this process. A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. We use a multidisciplinary approach, involving NMR, x-ray crystallography, surface plasmon resonance, mutagenesis, and in viv...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m111.236141

Authors


Mavridou, DA More by this author
Saridakis, E More by this author
Kritsiligkou, P More by this author
Goddard, AD More by this author
Stevens, JM More by this author
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Journal:
The Journal of biological chemistry
Volume:
286
Issue:
28
Pages:
24943-24956
Publication date:
2011-07-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:b5f634bc-a43c-4a44-9b9c-bec6307adfca
Source identifiers:
138824
Local pid:
pubs:138824

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