› 5b2n

X-ray diffraction
1.58Å resolution

Crystal structure of the light-driven chloride ion-pumping rhodopsin, ClP, from Nonlabens marinus

Released:
DOI: 10.2210/pdb5b2n/pdb
PDB entry 5b2n coloured by chain, front view.
PDB entry 5b2n coloured by chain, side view.
PDB entry 5b2n coloured by chain, top view.
Source organism: Nonlabens marinus S1-08
Primary publication:
Structural Mechanism for Light-driven Transport by a New Type of Chloride Ion Pump, Nonlabens marinus Rhodopsin-3.
Hosaka T, Yoshizawa S, Nakajima Y, Ohsawa N, Hato M, DeLong EF, Kogure K, Yokoyama S, Kimura-Someya T, Iwasaki W, Shirouzu M
J Biol Chem 291 17488-17495 (2016)
PMID: 27365396

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-197820 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chloride pumping rhodopsin Chain: A
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 30.71 KDa
Source organism: Nonlabens marinus S1-08
Expression system: Escherichia coli
UniProt:
  • Canonical: W8VZW3 (Residues: 1-272; Coverage: 100%)
Gene names: ClR, NMS_1267
Sequence domains: Bacteriorhodopsin-like protein
Structure domains: Rhodopsin 7-helix transmembrane proteins

Ligands and Environments

6 bound ligands:
Ligand RET 1 x RET
Ligand CL 1 x CL
Ligand HEX 2 x HEX
Ligand OCT 4 x OCT
Ligand D12 3 x D12
Ligand D10 3 x D10
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Spacegroup: C2
Unit cell:
a: 101.58Å b: 49.79Å c: 75.32Å
α: 90° β: 130.4° γ: 90°
R-values:
R R work R free
0.177 0.176 0.198
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications.
Govorunova et al. (2017)
3 more

6 mentions without citation

Conversion of microbial rhodopsins: insights into functionally essential elements and rational protein engineering.
Kaneko et al. (2017)
5 more