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

关键词：

D O I：

暂无

中图分类号：

学科分类号：

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.

引用

页码：573 / 577

页数：4

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