A two-domain elevator mechanism for sodium/proton antiport

Chiara Lee, Hae Joo Kang, Christoph von Ballmoos, Simon Newstead, Povilas Uzdavinys, David L. Dotson, So Iwata, Oliver Beckstein, Alexander D. Cameron () and David Drew ()
Additional contact information
Chiara Lee: Imperial College London, London SW7 2AZ, UK
Hae Joo Kang: Imperial College London, London SW7 2AZ, UK
Christoph von Ballmoos: Centre for Biomembrane Research, Stockholm University, SE-106 91 Stockholm, Sweden
Simon Newstead: Imperial College London, London SW7 2AZ, UK
Povilas Uzdavinys: Centre for Biomembrane Research, Stockholm University, SE-106 91 Stockholm, Sweden
David L. Dotson: Center for Biological Physics, Arizona State University
So Iwata: Imperial College London, London SW7 2AZ, UK
Oliver Beckstein: Center for Biological Physics, Arizona State University
Alexander D. Cameron: Imperial College London, London SW7 2AZ, UK
David Drew: Imperial College London, London SW7 2AZ, UK

Nature, 2013, vol. 501, issue 7468, 573-577

Abstract: The X-ray crystal structure of NapA, a Na+/H+ antiporter from Thermus thermophilus, in an active, outward-facing state is reported; comparisons to the structure of a related transporter in a low pH/inactivated, inward-facing state show the conformational changes that occur when the membrane protein moves from an inward-facing to an outward-facing state, suggesting that Na+/H+ antiporters operate by a two-domain rocking bundle model.

Date: 2013
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DOI: 10.1038/nature12484

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