- 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...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Publisher copy:
- 10.1073/pnas.0907315106
-
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- 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
- Language:
- English
- Keywords:
- Copyright holder:
- Pongprayoon et al.
- Copyright date:
- 2009
- Notes:
- Freely available online through the PNAS open access option.
Journal article
Simulations of anion transport through OprP reveal the molecular basis for high affinity and selectivity for phosphate.
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Thai Royal Government
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Biotechnology and Biological Sciences Research Council
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Wellcome Trust
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