 |
PDBsum entry 5g2c
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transport protein
|
PDB id
|
|
|
|
5g2c
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure and functional characterization of a light-Driven chloride pump having an ntq motif.
|
|
|
Authors
|
|
K.Kim,
S.K.Kwon,
S.H.Jun,
J.S.Cha,
H.Kim,
W.Lee,
J.F.Kim,
H.S.Cho.
|
|
|
Ref.
|
|
Nat Commun, 2016,
7,
12677.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
A novel light-driven chloride-pumping rhodopsin (ClR) containing an 'NTQ motif'
in its putative ion conduction pathway has been discovered and functionally
characterized in a genomic analysis study of a marine bacterium. Here we report
the crystal structure of ClR from the flavobacterium Nonlabens marinus S1-08(T)
determined under two conditions at 2.0 and 1.56 Å resolutions. The structures
reveal two chloride-binding sites, one around the protonated Schiff base and the
other on a cytoplasmic loop. We identify a '3 omega motif' formed by three
non-consecutive aromatic amino acids that is correlated with the B-C loop
orientation. Detailed ClR structural analyses with functional studies in E. coli
reveal the chloride ion transduction pathway. Our results help understand the
molecular mechanism and physiological role of ClR and provide a structural basis
for optogenetic applications.
|
|
|
|
|
|
|
