6S6C

Ground state structure of Archaerhodopsin-3 at 100K

6S6C の概要

• エントリーDOI: 10.2210/pdb6s6c/pdb
• 関連するPDBエントリー: 6GUX 6GUZ 6S63
• 分子名称: Archaerhodopsin-3, RETINAL, HEXADECANE, ... (9 entities in total)
• 機能のキーワード: membrane protein, rhodopsin, archaerhodopsin, retinal, lcp, synchrotron, cryo, proton transport
• 由来する生物種: Halorubrum sodomense
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28656.53

構造登録者

Moraes, I.,Judge, P.J.,Axford, D.,Kwan, T.O.C.,Bada Juarez, J.F.,Vinals, J.,Watts, A. (登録日: 2019-07-02, 公開日: 2020-07-22, 最終更新日: 2024-11-06)

主引用文献

Bada Juarez, J.F.,Judge, P.J.,Adam, S.,Axford, D.,Vinals, J.,Birch, J.,Kwan, T.O.C.,Hoi, K.K.,Yen, H.Y.,Vial, A.,Milhiet, P.E.,Robinson, C.V.,Schapiro, I.,Moraes, I.,Watts, A.
Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.
Nat Commun, 12:629-629, 2021

PubMed Abstract: Many transmembrane receptors have a desensitized state, in which they are unable to respond to external stimuli. The family of microbial rhodopsin proteins includes one such group of receptors, whose inactive or dark-adapted (DA) state is established in the prolonged absence of light. Here, we present high-resolution crystal structures of the ground (light-adapted) and DA states of Archaerhodopsin-3 (AR3), solved to 1.1 Å and 1.3 Å resolution respectively. We observe significant differences between the two states in the dynamics of water molecules that are coupled via H-bonds to the retinal Schiff Base. Supporting QM/MM calculations reveal how the DA state permits a thermodynamic equilibrium between retinal isomers to be established, and how this same change is prevented in the ground state in the absence of light. We suggest that the different arrangement of internal water networks in AR3 is responsible for the faster photocycle kinetics compared to homologs.

PubMed: 33504778
DOI: 10.1038/s41467-020-20596-0

実験手法

X-RAY DIFFRACTION (1.07 Å)