4IA4
Structure of the spinach aquaporin SoPIP2;1 at pH 6
Summary for 4IA4
Entry DOI | 10.2210/pdb4ia4/pdb |
Related | 1Z98 2B5F 3CLL 3CN5 3CN6 |
Descriptor | Aquaporin, MERCURY (II) ION (3 entities in total) |
Functional Keywords | integral membrane protein, aquaporin, water channel protein, transport protein |
Biological source | Spinacia oleracea (Spinach) |
Total number of polymer chains | 4 |
Total formula weight | 122126.34 |
Authors | Frick, A.,Jarva, M.,Tornroth-Horsefield, S. (deposition date: 2012-12-06, release date: 2013-05-29, Last modification date: 2024-11-13) |
Primary citation | Frick, A.,Jarva, M.,Tornroth-Horsefield, S. Structural basis for pH gating of plant aquaporins Febs Lett., 587:989-993, 2013 Cited by PubMed Abstract: 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. PubMed: 23454640DOI: 10.1016/j.febslet.2013.02.038 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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