› 3zgi

X-ray diffraction
2.25Å resolution

Crystal structure of the KRT10-binding region domain of the pneumococcal serine rich repeat protein PsrP

Released:
DOI: 10.2210/pdb3zgi/pdb
PDB entry 3zgi coloured by chain, front view.
PDB entry 3zgi coloured by chain, side view.
PDB entry 3zgi coloured by chain, top view.
Source organism: Streptococcus pneumoniae TIGR4
Primary publication:
The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.
Schulte T, Löfling J, Mikaelsson C, Kikhney A, Hentrich K, Diamante A, Ebel C, Normark S, Svergun D, Henriques-Normark B, Achour A
OpenAccess logo Open Biol 4 130090 (2014)
PMID: 24430336

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-493545 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pneumococcal serine-rich repeat protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 205 amino acids
Theoretical weight: 22.33 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A0A0H2URK1 (Residues: 187-385; Coverage: 4%)
Gene names: SP_1772, psrP
Structure domains: Immunoglobulin-like

Ligands and Environments

2 bound ligands:
Ligand SO4 6 x SO4
Ligand EDO 1 x EDO
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P41212
Unit cell:
a: 105.58Å b: 105.58Å c: 120.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.214
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins.
Kikhney et al. (2015)
3 more

2 mentions without citation

The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation.
Schulte et al. (2016)
1 more