› 1tn0

X-ray diffraction
2.5Å resolution

Structure of bacterorhodopsin mutant A51P

Released:
DOI: 10.2210/pdb1tn0/pdb
PDB entry 1tn0 coloured by chain, front view.
PDB entry 1tn0 coloured by chain, side view.
PDB entry 1tn0 coloured by chain, top view.
Source organism: Halobacterium salinarum
Primary publication:
Proline substitutions are not easily accommodated in a membrane protein.
Yohannan S, Yang D, Faham S, Boulting G, Whitelegge J, Bowie JU
J Mol Biol 341 1-6 (2004)
PMID: 15312757

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136411 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacteriorhodopsin Chains: A, B
Molecule details ›
Chains: A, B
Length: 249 amino acids
Theoretical weight: 26.96 KDa
Source organism: Halobacterium salinarum
Expression system: Escherichia coli
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 2 x RET
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 45.105Å b: 108.582Å c: 55.821Å
α: 90° β: 113.74° γ: 90°
R-values:
R R work R free
0.177 0.173 0.262
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs.
Senes et al. (2004)
4 more

2 mentions without citation

'Hot' macromolecular crystals.
Koclega et al. (2009)
1 more