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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


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:
2009-12-01
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
Source identifiers:
100400
Language:
English
Keywords:
Pubs id:
pubs:100400
UUID:
uuid:8fd9d80a-b800-4b72-af3a-4b81d6a75b38
Local pid:
pubs:100400
Deposit date:
2012-12-19

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