- Abstract:
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Multidrug and toxic compound extrusion (MATE) transporters exist in all three domains of life. They confer multidrug resistance by utilizing H+ or Na+ electrochemical gradients to extrude various drugs across the cell membranes. The substrate binding and the transport mechanism of MATE transporters is a fundamental process but so far not fully understood. Here we report a detailed substrate binding study of NorM_PS, a representative MATE transporter from Pseudomonas stutzeri. Our results indi...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 1.8MB)
-
- Publisher copy:
- 10.1074/jbc.M116.728618
-
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- Publisher:
- American Society for Biochemistry and Molecular Biology Publisher's website
- Journal:
- Journal of Biological Chemistry Journal website
- Volume:
- 291
- Issue:
- 30
- Pages:
- 15503-15514
- Publication date:
- 2016-07-22
- DOI:
- EISSN:
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1083-351X
- ISSN:
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0021-9258
- Pubs id:
-
pubs:719898
- URN:
-
uri:f74d5ee7-49cf-4fac-8838-d8125ac2b3c1
- UUID:
-
uuid:f74d5ee7-49cf-4fac-8838-d8125ac2b3c1
- Local pid:
- pubs:719898
- Copyright holder:
- American Society for Biochemistry and Molecular Biology, Inc.
- Copyright date:
- 2016
- Notes:
- Copyright © 2016 by The American Society for Biochemistry and Molecular Biology, Inc.
Journal article
Identification of the high-affinity substrate-binding site of the multidrug and toxic compound extrusion (MATE) family transporter from Pseudomonas stutzeri
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Max-Planck-Gesellschaft
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Deutsche Forschungsgemeinschaft
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Cluster of Excellence Frankfurt on Macromolecular Complexes Frankfurt and CRC 807
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