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

Journal article

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...

Expand abstract

Authors: Marcoux, J; Politis, A; Rinehart, D; Marshall, D; Wallace, M

• Publisher: Cell Press
• Journal: Structure
• Volume: 22
• Issue: 5
• Pages: 781-790
• Publication date: 2014-05-06
• DOI: 10.1016/j.str.2014.03.004
• EISSN: 1878-4186
• ISSN: 0969-2126
• Language: English