1Z98

Crystal structure of the spinach aquaporin SoPIP2;1 in a closed conformation

1Z98 の概要

• エントリーDOI: 10.2210/pdb1z98/pdb
• 分子名称: aquaporin, CADMIUM ION (3 entities in total)
• 機能のキーワード: integral membrane protein; pip; alpha-helical; aquaporin, transport protein, membrane protein
• 由来する生物種: Spinacia oleracea (spinach)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60084.45

構造登録者

Tornroth-Horsefield, S.,Hedfalk, K.,Johanson, U.,Karlsson, M.,Neutze, R.,Kjellbom, P. (登録日: 2005-04-01, 公開日: 2005-12-20, 最終更新日: 2024-11-20)

主引用文献

Tornroth-Horsefield, S.,Wang, Y.,Hedfalk, K.,Johanson, U.,Karlsson, M.,Tajkhorshid, E.,Neutze, R.,Kjellbom, P.
Structural mechanism of plant aquaporin gating
Nature, 439:688-694, 2006

PubMed Abstract: Plants counteract fluctuations in water supply by regulating all aquaporins in the cell plasma membrane. Channel closure results either from the dephosphorylation of two conserved serine residues under conditions of drought stress, or from the protonation of a conserved histidine residue following a drop in cytoplasmic pH due to anoxia during flooding. Here we report the X-ray structure of the spinach plasma membrane aquaporin SoPIP2;1 in its closed conformation at 2.1 A resolution and in its open conformation at 3.9 A resolution, and molecular dynamics simulations of the initial events governing gating. In the closed conformation loop D caps the channel from the cytoplasm and thereby occludes the pore. In the open conformation loop D is displaced up to 16 A and this movement opens a hydrophobic gate blocking the channel entrance from the cytoplasm. These results reveal a molecular gating mechanism which appears conserved throughout all plant plasma membrane aquaporins.

PubMed: 16340961
DOI: 10.1038/nature04316

実験手法

X-RAY DIFFRACTION (2.1 Å)