› 5ij3

X-ray diffraction
1.7Å resolution

SrpA adhesin in complex with sialyl T antigen

Released:
DOI: 10.2210/pdb5ij3/pdb
PDB entry 5ij3 coloured by chain, front view.
PDB entry 5ij3 coloured by chain, side view.
PDB entry 5ij3 coloured by chain, top view.
Source organism: Streptococcus sanguinis SK36
Primary publication:
Structures of the Streptococcus sanguinis SrpA Binding Region with Human Sialoglycans Suggest Features of the Physiological Ligand.
Loukachevitch LV, Bensing BA, Yu H, Zeng J, Chen X, Sullam PM, Iverson TM
Biochemistry 55 5927-5937 (2016)
PMID: 27685666

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106994 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Gram-positive cocci surface proteins LPxTG domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 197 amino acids
Theoretical weight: 21.5 KDa
Source organism: Streptococcus sanguinis SK36
Expression system: Escherichia coli
UniProt:
  • Canonical: A3CM52 (Residues: 252-448; Coverage: 12%)
Gene names: SSA_0829, srpA
Sequence domains:
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

Carbohydrate polymer : NEW Components: A2G, GAL, SIA
Carbohydrate polymer
2 bound ligands:
Ligand CA 7 x CA
Ligand ACT 6 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: C2
Unit cell:
a: 173.911Å b: 46.766Å c: 65.169Å
α: 90° β: 102.73° γ: 90°
R-values:
R R work R free
0.187 0.186 0.207
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Streptococcus sanguinis biofilm formation & interaction with oral pathogens.
Zhu et al. (2018)
3 more

1 mention without citation

Structures of the Streptococcus sanguinis SrpA Binding Region with Human Sialoglycans Suggest Features of the Physiological Ligand.
Loukachevitch et al. (2016)