› 4ff5

X-ray diffraction
1.86Å resolution

Structure basis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus pneumoniae participating in host cell invasion

Released:
DOI: 10.2210/pdb4ff5/pdb
PDB entry 4ff5 coloured by chain, front view.
PDB entry 4ff5 coloured by chain, side view.
PDB entry 4ff5 coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Structural basis of the novel S. pneumoniae virulence factor, GHIP, a glycosyl hydrolase 25 participating in host-cell invasion.
Niu S, Luo M, Tang J, Zhou H, Zhang Y, Min X, Cai X, Zhang W, Xu W, Li D, Ding J, Hu Y, Wang D, Huang A, Yin Y, Wang D
PLoS One 8 e68647 (2013)
PMID: 23874703

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-101432 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 30.09 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A0A0H2UPQ2 (Residues: 1-266; Coverage: 100%)
Gene name: SP_0987
Sequence domains: Glycosyl hydrolases family 25
Structure domains: Glycosidases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 36.46Å b: 40.88Å c: 147.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.18 0.244
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Review: current and new generation pneumococcal vaccines.
Feldman et al. (2014)
6 other articles

3 mentions without citation

Biochemical characterization of the major N-acetylmuramidase from Lactobacillus buchneri.
Anzengruber et al. (2014)
2 more