› 4ov0

X-ray diffraction
2Å resolution

Structure of Bacteriorhdopsin Transferred from Amphipol A8-35 to a Lipidic Mesophase

Released:
DOI: 10.2210/pdb4ov0/pdb
PDB entry 4ov0 coloured by chain, front view.
PDB entry 4ov0 coloured by chain, side view.
PDB entry 4ov0 coloured by chain, top view.
Source organism: Halobacterium salinarum NRC-1
Primary publication:
High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase.
Polovinkin V, Gushchin I, Sintsov M, Round E, Balandin T, Chervakov P, Shevchenko V, Utrobin P, Popov A, Borshchevskiy V, Mishin A, Kuklin A, Willbold D, Chupin V, Popot JL, Gordeliy V
J Membr Biol 247 997-1004 (2014)
PMID: 25192977

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136413 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacteriorhodopsin Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 26.93 KDa
Source organism: Halobacterium salinarum NRC-1
UniProt:
  • Canonical: P02945 (Residues: 14-262; Coverage: 95%)
Gene names: VNG_1467G, bop
Sequence domains: Bacteriorhodopsin-like protein
Structure domains: Rhodopsin 7-helix transmembrane proteins

Ligands and Environments

1 bound ligand:
Ligand RET 1 x RET
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P63
Unit cell:
a: 60.999Å b: 60.999Å c: 108.174Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.179 0.209

Quick links

Citations

6 review citations

Amphipols for each season.
Zoonens et al. (2014)
5 more

1 mention without citation

Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments.
Puthenveetil et al. (2019)