4QK7

Influenza A M2 wild type TM domain at high pH in the lipidic cubic phase under cryo diffraction conditions

4QK7 の概要

• エントリーDOI: 10.2210/pdb4qk7/pdb
• 関連するPDBエントリー: 4QK6 4QKC 4QKL 4QKM
• 分子名称: influenza M2 monomer, CALCIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: transmembrane alpha helix, ph-activated proton channel, viral protein
• 由来する生物種: Influenza A virus
• 細胞内の位置: Virion membrane : W8PGZ1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3645.10

構造登録者

Thomaston, J.L. (登録日: 2014-06-05, 公開日: 2015-11-11, 最終更新日: 2024-11-06)

主引用文献

Thomaston, J.L.,Alfonso-Prieto, M.,Woldeyes, R.A.,Fraser, J.S.,Klein, M.L.,Fiorin, G.,DeGrado, W.F.
High-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transduction.
Proc.Natl.Acad.Sci.USA, 112:14260-14265, 2015

PubMed Abstract: The matrix 2 (M2) protein from influenza A virus is a proton channel that uses His37 as a selectivity filter. Here we report high-resolution (1.10 Å) cryogenic crystallographic structures of the transmembrane domain of M2 at low and high pH. These structures reveal that waters within the pore form hydrogen-bonded networks or "water wires" spanning 17 Å from the channel entrance to His37. Pore-lining carbonyl groups are well situated to stabilize hydronium via second-shell interactions involving bridging water molecules. In addition, room temperature crystallographic structures indicate that water becomes increasingly fluid with increasing temperature and decreasing pH, despite the higher electrostatic field. Complementary molecular dynamics simulations reveal a collective switch of hydrogen bond orientations that can contribute to the directionality of proton flux as His37 is dynamically protonated and deprotonated in the conduction cycle.

PubMed: 26578770
DOI: 10.1073/pnas.1518493112

実験手法

X-RAY DIFFRACTION (1.1 Å)