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Simulations of anion transport through OprP reveal the molecular basis for high affinity and selectivity for phosphate.

Abstract:

The outer membrane protein OprP from Pseudomonas aeruginosa forms a phosphate selective pore. To understand the mechanism of phosphate permeation and selectivity, we used three simulation techniques [equilibrium molecular dynamics simulations, steered molecular dynamics, and calculation of a potential of mean force (PMF)]. The PMF for phosphate reveals a deep free energy well midway along the OprP channel. Two adjacent phosphate-binding sites (W1 and W2), each with a well depth of approximate...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1073/pnas.0907315106

Authors


Pongprayoon, P More by this author
Beckstein, O More by this author
Sansom, MS More by this author
Thai Royal Government More from this funder
Biotechnology and Biological Sciences Research Council More from this funder
Wellcome Trust More from this funder
Publisher:
National Academy of Sciences Publisher's website
Journal:
Proceedings of the National Academy of Sciences of the United States of America Journal website
Volume:
106
Issue:
51
Pages:
21614-21618
Publication date:
2009-12-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:8fd9d80a-b800-4b72-af3a-4b81d6a75b38
Source identifiers:
100400
Local pid:
pubs:100400

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