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Structural basis for pH gating of plant aquaporins
Author(s) -
Frick Anna,
Järvå Michael,
Törnroth-Horsefield Susanna
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.02.038
Subject(s) - aquaporin , gating , biophysics , histidine , chemistry , membrane , cytosol , biochemistry , biology , enzyme , amino acid
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.