6JYA

Structure of dark-state marine bacterial chloride importer, NM-R3, with CW laser (ND-10%) at 95K.

6JYA の概要

• エントリーDOI: 10.2210/pdb6jya/pdb
• 分子名称: Chloride pumping rhodopsin, RETINAL, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: photo-excitation, chloride pump, retinal, membrane protein
• 由来する生物種: Nonlabens marinus S1-08
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36375.85

構造登録者

Yun, J.H.,Ohki, M.,Park, S.Y.,Lee, W. (登録日: 2019-04-26, 公開日: 2020-03-04, 最終更新日: 2024-11-06)

主引用文献

Yun, J.H.,Ohki, M.,Park, J.H.,Ishimoto, N.,Sato-Tomita, A.,Lee, W.,Jin, Z.,Tame, J.R.H.,Shibayama, N.,Park, S.Y.,Lee, W.
Pumping mechanism of NM-R3, a light-driven bacterial chloride importer in the rhodopsin family.
Sci Adv, 6:eaay2042-eaay2042, 2020

PubMed Abstract: A newly identified microbial rhodopsin, NM-R3, from the marine flavobacterium , was recently shown to drive chloride ion uptake, extending our understanding of the diversity of mechanisms for biological energy conversion. To clarify the mechanism underlying its function, we characterized the crystal structures of NM-R3 in both the dark state and early intermediate photoexcited states produced by laser pulses of different intensities and temperatures. The displacement of chloride ions at five different locations in the model reflected the detailed anion-conduction pathway, and the activity-related key residues-Cys, Ser, Gln, and Phe-were identified by mutation assays and spectroscopy. Comparisons with other proteins, including a closely related outward sodium ion pump, revealed key motifs and provided structural insights into light-driven ion transport across membranes by the NQ subfamily of rhodopsins. Unexpectedly, the response of the retinal in NM-R3 to photostimulation appears to be substantially different from that seen in bacteriorhodopsin.

PubMed: 32083178
DOI: 10.1126/sciadv.aay2042

実験手法

X-RAY DIFFRACTION (1.803 Å)