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Identification of the high-affinity substrate-binding site of the multidrug and toxic compound extrusion (MATE) family transporter from Pseudomonas stutzeri

Abstract:

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...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1074/jbc.M116.728618

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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
H9 STRUCTURAL GENOMICS CONSORTIUM
Role:
Author
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Max-Planck-Gesellschaft More from this funder
Deutsche Forschungsgemeinschaft More from this funder
Cluster of Excellence Frankfurt on Macromolecular Complexes Frankfurt and CRC 807 More from this funder
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:
1083-351X
ISSN:
0021-9258
Pubs id:
pubs:719898
URN:
uri:f74d5ee7-49cf-4fac-8838-d8125ac2b3c1
UUID:
uuid:f74d5ee7-49cf-4fac-8838-d8125ac2b3c1
Local pid:
pubs:719898

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