Structure of a cation-bound multidrug and toxic compound extrusion transporter

Xiao He, Paul Szewczyk, Andrey Karyakin, Mariah Evin, Wen-Xu Hong, Qinghai Zhang and Geoffrey Chang ()
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Xiao He: The Scripps Research Institute, 10550 North Torrey Pines Road, CB105, La Jolla, California 92037, USA
Paul Szewczyk: The Scripps Research Institute, 10550 North Torrey Pines Road, CB105, La Jolla, California 92037, USA
Andrey Karyakin: The Scripps Research Institute, 10550 North Torrey Pines Road, CB105, La Jolla, California 92037, USA
Mariah Evin: The Scripps Research Institute, 10550 North Torrey Pines Road, CB105, La Jolla, California 92037, USA
Wen-Xu Hong: The Scripps Research Institute, 10550 North Torrey Pines Road, CB105, La Jolla, California 92037, USA
Qinghai Zhang: The Scripps Research Institute, 10550 North Torrey Pines Road, CB105, La Jolla, California 92037, USA
Geoffrey Chang: The Scripps Research Institute, 10550 North Torrey Pines Road, CB105, La Jolla, California 92037, USA

Nature, 2010, vol. 467, issue 7318, 991-994

Abstract: MATE transporter structure Transporter proteins from the MATE (multidrug and toxic compound extrusion) family are involved in metabolite transport in plants and in multidrug resistance in bacteria and mammals. MATE transporters were the only remaining class of multidrug resistance transporter whose structure was not known. The X-ray structure of a prototypical MATE protein, NorM from Vibrio cholerae, has now been determined to 3.65 Å resolution, revealing a protein topology distinct from other membrane-protein structures solved to date. The structure is in an 'outward-facing' conformation, with a cation-binding site in close proximity to residues previously deemed critical for transport.

Date: 2010
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DOI: 10.1038/nature09408

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