3ZOJ

High-resolution structure of Pichia Pastoris aquaporin Aqy1 at 0.88 A

3ZOJ の概要

• エントリーDOI: 10.2210/pdb3zoj/pdb
• 分子名称: AQUAPORIN, octyl beta-D-glucopyranoside, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: channel, membrane protein
• 由来する生物種: KOMAGATAELLA PASTORIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30915.90

構造登録者

Kosinska-Eriksson, U.,Fischer, G.,Friemann, R.,Enkavi, G.,Tajkhorshid, E.,Neutze, R. (登録日: 2013-02-21, 公開日: 2013-06-26, 最終更新日: 2023-12-20)

主引用文献

Kosinska-Eriksson, U.,Fischer, G.,Friemann, R.,Enkavi, G.,Tajkhorshid, E.,Neutze, R.
Subangstrom Resolution X-Ray Structure Details Aquaporin-Water Interactions
Science, 340:1346-, 2013

PubMed Abstract: Aquaporins are membrane channels that facilitate the flow of water across biological membranes. Two conserved regions are central for selective function: the dual asparagine-proline-alanine (NPA) aquaporin signature motif and the aromatic and arginine selectivity filter (SF). Here, we present the crystal structure of a yeast aquaporin at 0.88 angstrom resolution. We visualize the H-bond donor interactions of the NPA motif's asparagine residues to passing water molecules; observe a polarized water-water H-bond configuration within the channel; assign the tautomeric states of the SF histidine and arginine residues; and observe four SF water positions too closely spaced to be simultaneously occupied. Strongly correlated movements break the connectivity of SF waters to other water molecules within the channel and prevent proton transport via a Grotthuss mechanism.

PubMed: 23766328
DOI: 10.1126/SCIENCE.1234306

実験手法

X-RAY DIFFRACTION (0.88 Å)