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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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Publication status:
Published

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Publisher copy:
10.1016/j.str.2014.03.004

Authors


Marcoux, J More by this author
Politis, A More by this author
Rinehart, D More by this author
Marshall, DP More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
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Journal:
Structure (London, England : 1993)
Volume:
22
Issue:
5
Pages:
781-790
Publication date:
2014-05-05
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:2b7d2d4e-15da-4801-8167-220298ff8d6b
Source identifiers:
463112
Local pid:
pubs:463112
Language:
English

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