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: 2023-11-08)

Primary citation

Frick, A.,Jarva, M.,Tornroth-Horsefield, S.
Structural basis for pH gating of plant aquaporins
Febs Lett., 587:989-993, 2013

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: 23454640
DOI: 10.1016/j.febslet.2013.02.038

Experimental method

X-RAY DIFFRACTION (3.1 Å)