Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter

Romina Mancusso, G. Glenn Gregorio, Qun Liu and Da-Neng Wang ()
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Romina Mancusso: The Helen L. and Martin S. Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, New York, New York 10016, USA
G. Glenn Gregorio: The Helen L. and Martin S. Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, New York, New York 10016, USA
Qun Liu: New York Structural Biology Center, NSLS X4, Brookhaven National Laboratory, Upton, New York 11973, USA
Da-Neng Wang: The Helen L. and Martin S. Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, New York, New York 10016, USA

Nature, 2012, vol. 491, issue 7425, 622-626

Abstract: The cytosolic concentration of citrate partially depends on its direct import across the plasma membrane by the Na+-dependent citrate transporter (NaCT); here the X-ray crystal structure of a bacterial homologue of NaCT is reported, which, along with transport-activity studies, suggests how specific conformational changes facilitate substrate translocation across the cellular membrane.

Date: 2012
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DOI: 10.1038/nature11542

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