› 2v04

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE

Released:
DOI: 10.2210/pdb2v04/pdb
PDB entry 2v04 coloured by chain, front view.
PDB entry 2v04 coloured by chain, side view.
PDB entry 2v04 coloured by chain, top view.
Source organism: Streptococcus pneumoniae R6
Primary publication:
Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae.
Molina R, González A, Stelter M, Pérez-Dorado I, Kahn R, Morales M, Moscoso M, Campuzano S, Campillo NE, Mobashery S, García JL, García P, Hermoso JA
EMBO Rep 10 246-51 (2009)
PMID: 19165143

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184164 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Choline-binding protein F Chain: A
Molecule details ›
Chain: A
Length: 311 amino acids
Theoretical weight: 36.32 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8DR52 (Residues: 28-338; Coverage: 100%)
Gene names: cbpF, spr0337
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21212
Unit cell:
a: 52.397Å b: 115.792Å c: 72.985Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.25
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Lipoteichoic acid synthesis and function in gram-positive bacteria.
Percy et al. (2014)
6 more

6 mentions without citation

Choline Binding Proteins from Streptococcus pneumoniae: A Dual Role as Enzybiotics and Targets for the Design of New Antimicrobials.
Maestro et al. (2016)
5 more