9H20

Continuous dark state structure of Sensory Rhodopsin II solved by serial millisecond crystallography

「7PNC」から置き換えられました

9H20 の概要

• エントリーDOI: 10.2210/pdb9h20/pdb
• 関連するPDBエントリー: 8PWP 9H1W 9H1X
• 分子名称: Sensory rhodopsin-2, RETINAL, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: srii, serial millisecond crystallography, sensory rhodopsin, sensory rhodopsin ii, smx, ssx, signaling protein
• 由来する生物種: Natronomonas pharaonis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31464.22

構造登録者

Ortolani, G.,Bosman, R.,Branden, G.,Neutze, R. (登録日: 2024-10-10, 公開日: 2025-04-30, 最終更新日: 2025-05-28)

主引用文献

Bosman, R.,Ortolani, G.,Ghosh, S.,James, D.,Norder, P.,Hammarin, G.,Ulfarsdottir, T.B.,Ostojic, L.,Weinert, T.,Dworkowski, F.,Tomizaki, T.,Standfuss, J.,Branden, G.,Neutze, R.
Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.
Nat Commun, 16:3460-3460, 2025

PubMed Abstract: Microbial rhodopsins form a diverse family of light-sensitive seven-transmembrane helix retinal proteins that function as active proton or ion pumps, passive light-gated ion channels, and photosensors. To understand how light-sensing in archaea is initiated by sensory rhodopsins, we perform serial synchrotron X-ray crystallography (SSX) studies of light induced conformational changes in sensory rhodopsin II (NpSRII) from the archaea Natronomonas pharaonis, both collecting time-resolved SSX data and collecting SSX data during continuous illumination. Comparing light-induced electron density changes in NpSRII with those reported for bacteriorhodopsin (bR) reveals several common light-induced structural perturbations. Unlike bR, however, helix G of NpSRII does not unwind near the conserved lysine residue to which retinal is covalently bound and therefore transient water molecule binding sites do not arise immediately to the cytoplasmic side of retinal. These structural differences prolong the duration of the NpSRII photocycle relative to bR, allowing time for the light-initiated sensory signal to be amplified.

PubMed: 40216733
DOI: 10.1038/s41467-025-58263-x

実験手法

X-RAY DIFFRACTION (2.2 Å)