Structure and mechanism of a glutamate–GABA antiporter

Dan Ma, Peilong Lu, Chuangye Yan, Chao Fan, Ping Yin, Jiawei Wang and Yigong Shi ()
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Dan Ma: Ministry of Education Protein Science Laboratory, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Peilong Lu: Ministry of Education Protein Science Laboratory, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Chuangye Yan: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Chao Fan: Ministry of Education Protein Science Laboratory, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Ping Yin: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Jiawei Wang: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University
Yigong Shi: Ministry of Education Protein Science Laboratory, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University

Nature, 2012, vol. 483, issue 7391, 632-636

Abstract: The X-ray crystal structure of the glutamate–GABA antiporter GadC is determined, revealing an inward-open conformation and providing insights into mechanism of amino acid antiport that is needed for acid resistance in bacteria.

Date: 2012
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DOI: 10.1038/nature10917

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