期刊
FEBS LETTERS
卷 587, 期 7, 页码 989-993出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2013.02.038
关键词
Membrane protein; Aquaporin; Plasma membrane intrinsic protein; pH gating; X-ray crystallography
资金
- Swedish Research Council
Plants have evolved to cope with fluctuations in water supply by gating their water channels known as aquaporins. During flooding, a rapid drop of cytosolic pH due to anoxia leads to a simultaneous closure of the aquaporins in the plasma membrane. The closing mechanism has been suggested to involve a conserved histidine on cytosolic loop D. Here we report the crystal structure of a spinach aquaporin at low pH, revealing for the first time the structural basis for how this pH-sensitive histidine helps to keep the aquaporin in a closed state. (c) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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