› 4ryq

X-ray diffraction
1.7Å resolution

Crystal structure of BcTSPO, type 2 at 1.7 Angstrom

Released:
DOI: 10.2210/pdb4ryq/pdb
PDB entry 4ryq coloured by chain, front view.
PDB entry 4ryq coloured by chain, side view.
PDB entry 4ryq coloured by chain, top view.
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)
Assembly name:
PDBe Complex ID:
PDB-CPX-182483 (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

30 review citations

Neuroinflammation in Neurodegenerative Disorders-a Review.
Schain et al. (2017)
29 more

8 mentions without citation

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