The mechanism of sodium and substrate release from the binding pocket of vSGLT

Akira Watanabe, Seungho Choe, Vincent Chaptal, John M. Rosenberg, Ernest M. Wright, Michael Grabe () and Jeff Abramson ()
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Akira Watanabe: University of California, Los Angeles
Seungho Choe: University of Pittsburgh
Vincent Chaptal: University of California, Los Angeles
John M. Rosenberg: University of Pittsburgh
Ernest M. Wright: University of California, Los Angeles
Michael Grabe: University of Pittsburgh
Jeff Abramson: University of California, Los Angeles

Nature, 2010, vol. 468, issue 7326, 988-991

Abstract: Sodium-coupled transport In membrane proteins with a 'LeuT-fold', it is not clear how ion- and substrate-transport are coupled. Watanabe et al. present a comprehensive study of the structure and biochemical properties of the sodium/galactose transporter (vSGLT) from Vibrio parahaemolyticus, and a new crystal structure of the 'inward-open' conformation. These experiments show that sodium exit causes a reorientation of transmembrane helix 1, opening an inner gate required for substrate exit, while also triggering minor rigid body movements in two sets of transmembrane helical bundles. This cascade of conformational changes is responsible for the proper timing of ion and substrate release.

Date: 2010
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DOI: 10.1038/nature09580

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