4ia4 | pdb_00004ia4

Structure of the spinach aquaporin SoPIP2;1 at pH 6

spinqualitylabelsall models 4ia4, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ia4 is a 4 chain structure with sequence from Spiol. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HG Related: 1z98, 2b5f, 3cll, 3cn5, 3cn6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Structural basis for pH gating of plant aquaporins.,Frick A, Jarva M, Tornroth-Horsefield S FEBS Lett. 2013 Apr 2;587(7):989-93. doi: 10.1016/j.febslet.2013.02.038. Epub, 2013 Feb 27. PMID:23454640 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aquaporin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA