› 3pnt

X-ray diffraction
2.8Å resolution

Crystal Structure of the Streptococcus pyogenes NAD+ glycohydrolase SPN in complex with IFS, the Immunity Factor for SPN

Released:
DOI: 10.2210/pdb3pnt/pdb
Model geometry
Fit model/data
PDB entry 3pnt coloured by chain, front view.
PDB entry 3pnt coloured by chain, side view.
PDB entry 3pnt coloured by chain, top view.
Source organism: Streptococcus pyogenes
Primary publication:
Structural basis of Streptococcus pyogenes immunity to its NAD+ glycohydrolase toxin.
Smith CL, Ghosh J, Elam JS, Pinkner JS, Hultgren SJ, Caparon MG, Ellenberger T
Structure 19 192-202 (2011)
PMID: 21300288

Function and Biology Details

Reaction catalysed: 
NAD(+) + H(2)O = ADP-D-ribose + nicotinamide
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112875 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nicotine adenine dinucleotide glycohydrolase catalytic domain-containing protein Chains: A, C
Molecule details ›
Chains: A, C
Length: 268 amino acids
Theoretical weight: 31.17 KDa
Source organism: Streptococcus pyogenes
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: D7S065 (Residues: 191-451; Coverage: 62%)
Gene name: spn
Sequence domains: NAD glycohydrolase catalytic domain
Structure domains: Nicotine adenine dinucleotide glycohydrolase, helical linker domain
Immunity factor for SPN Chains: B, D
Molecule details ›
Chains: B, D
Length: 161 amino acids
Theoretical weight: 19.21 KDa
Source organism: Streptococcus pyogenes
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q2VJ58 (Residues: 1-161; Coverage: 100%)
Gene names: E0F66_06230, ifs
Sequence domains: Immunity factor for SPN
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2
Unit cell:
a: 198.817Å b: 57.892Å c: 89.699Å
α: 90° β: 107.2° γ: 90°
R-values:
R R work R free
0.212 0.208 0.278
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

The natural history of ADP-ribosyltransferases and the ADP-ribosylation system.
Aravind et al. (2015)
1 more

6 mentions without citation

Analysis of polymorphic residues reveals distinct enzymatic and cytotoxic activities of the Streptococcus pyogenes NAD+ glycohydrolase.
Chandrasekaran et al. (2013)
5 more