A two-domain elevator mechanism for sodium/proton antiport

被引：0
|
作者：
Chiara Lee
Hae Joo Kang
Christoph von Ballmoos
Simon Newstead
Povilas Uzdavinys
David L. Dotson
So Iwata
Oliver Beckstein
Alexander D. Cameron
David Drew
机构：
[1] Imperial College London,Division of Molecular Biosciences
[2] London SW7 2AZ,Department of Biochemistry and Biophysics
[3] UK,Department of Physics
[4] Centre for Biomembrane Research,undefined
[5] Stockholm University,undefined
[6] SE-106 91 Stockholm,undefined
[7] Sweden,undefined
[8] Center for Biological Physics,undefined
[9] Arizona State University,undefined
[10] Membrane Protein Laboratory,undefined
[11] Diamond Light Source,undefined
[12] Harwell Science and Innovation Campus,undefined
[13] Didcot,undefined
[14] Chilton,undefined
[15] Oxfordshire OX11 0DE,undefined
[16] UK,undefined
[17] Research Complex at Harwell Rutherford,undefined
[18] Appleton Laboratory,undefined
[19] Harwell,undefined
[20] Oxford,undefined
[21] Didcot,undefined
[22] Oxfordshire OX11 0FA,undefined
[23] UK,undefined
[24] School of Life Sciences,undefined
[25] University of Warwick,undefined
[26] Gibbet Hill Road,undefined
[27] Coventry CV4 7AL,undefined
[28] UK,undefined
[29] Present address: Department of Biochemistry,undefined
[30] University of Oxford,undefined
[31] South Parks Road,undefined
[32] Oxford OX1 3QU,undefined
[33] UK.,undefined
来源：
Nature | 2013年 / 501卷
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摘要：
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.
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页码：573 / 577
页数：4
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