› 4ryq

X-ray diffraction
1.7Å resolution

Crystal structure of BcTSPO, type 2 at 1.7 Angstrom

Released:
DOI: 10.2210/pdb4ryq/pdb
PDB 4ryq coloured by chain and viewed from the front.
PDB 4ryq coloured by chain and viewed from the side.
PDB 4ryq coloured by chain and viewed from the top.
Source organism: Bacillus cereus ATCC 14579
Primary publication:
Protein structure. Structure and activity of tryptophan-rich TSPO proteins.
Guo Y, Kalathur RC, Liu Q, Kloss B, Bruni R, Ginter C, Kloppmann E, Rost B, Hendrickson WA
Science 347 551-5 (2015)
PMID: 25635100

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan-rich protein TspO Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 21.5 KDa
Source organism: Bacillus cereus ATCC 14579
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q81BL7 (Residues: 1-153; Coverage: 100%)
Gene names: BC_3136, tspO
Sequence domains: TspO/MBR family

Ligands and Environments

1 bound ligand:
Ligand MPG 7 x MPG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P212121
Unit cell:
a: 28.714Å b: 54.618Å c: 106.905Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.224 0.247
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

26 review citations

Cellular sources of TSPO expression in healthy and diseased brain.
Nutma et al. (2021)
25 more

8 mentions without citation

Insight into the Structural Features of TSPO: Implications for Drug Development.
Lacapere et al. (2020)
7 more