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Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA

Abstract:

The transmembrane domain of the outer membrane protein A (OmpA) from Escherichia coli is an excellent model for structural and folding studies of β-barrel membrane proteins. However, full-length OmpA resists crystallographic efforts, and the link between its function and tertiary structure remains controversial. Here we use site-directed mutagenesis and mass spectrometry of different constructs of OmpA, released in the gas phase from detergent micelles, to define the minimal region encompassi...

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Publisher copy:
10.1016/j.str.2014.03.004

Authors


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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Role:
Author
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Publisher:
Cell Press
Journal:
Structure
Volume:
22
Issue:
5
Pages:
781-790
Publication date:
2014-05-06
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:52c53b1f-a1f9-473c-97d1-c6c6c87d1606
Source identifiers:
466540
Local pid:
pubs:466540
Language:
English

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