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Dynamics of a bacterial multidrug ABC transporter in the inward- and outward-facing conformations.

Abstract:

The study of membrane proteins remains a challenging task, and approaches to unravel their dynamics are scarce. Here, we applied hydrogen/deuterium exchange (HDX) coupled to mass spectrometry to probe the motions of a bacterial multidrug ATP-binding cassette (ABC) transporter, BmrA, in the inward-facing (resting state) and outward-facing (ATP-bound) conformations. Trypsin digestion and global or local HDX support the transition between inward- and outward-facing conformations during the catal...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.1204067109

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Role:
Author
Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
109
Issue:
27
Pages:
10832-10836
Publication date:
2012-07-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:9752f355-5772-484d-9582-0b65b207ec69
Source identifiers:
344613
Local pid:
pubs:344613

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