6JY8

Structure of dark-state marine bacterial chloride importer, NM-R3, with CW laser (ND-3%) at 95K.

Summary for 6JY8

• Entry DOI: 10.2210/pdb6jy8/pdb
• Descriptor: Chloride pumping rhodopsin, RETINAL, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: photo-excitation, chloride pump, retinal, membrane protein
• Biological source: Nonlabens marinus S1-08
• Total number of polymer chains: 1
• Total formula weight: 36375.85

Authors

Yun, J.H.,Ohki, M.,Park, S.Y.,Lee, W. (deposition date: 2019-04-26, release date: 2020-03-04, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)