› 3pnd

X-ray diffraction
2.75Å resolution

FAD binding by ApbE protein from Salmonella enterica: a new class of FAD binding proteins

Released:
DOI: 10.2210/pdb3pnd/pdb
PDB entry 3pnd coloured by chain, front view.
PDB entry 3pnd coloured by chain, side view.
PDB entry 3pnd coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
FAD binding by ApbE protein from Salmonella enterica: a new class of FAD-binding proteins.
Boyd JM, Endrizzi JA, Hamilton TL, Christopherson MR, Mulder DW, Downs DM, Peters JW
J Bacteriol 193 887-95 (2011)
PMID: 21148731

Function and Biology Details

Reaction catalysed: 
FAD + [protein]-L-threonine = [protein]-FMN-L-threonine + AMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154429 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD:protein FMN transferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 337 amino acids
Theoretical weight: 36.99 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P41780 (Residues: 21-350; Coverage: 100%)
Gene names: STM2266, apbE
Sequence domains: ApbE family
Structure domains: ApbE-like domains

Ligands and Environments

2 bound ligands:
Ligand SO4 44 x SO4
Ligand FAD 4 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 65.103Å b: 120.85Å c: 212.058Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.202 0.254
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Flavin transferase: the maturation factor of flavin-containing oxidoreductases.
Bogachev et al. (2018)
15 other articles

5 mentions without citation

Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins.
Bertsova et al. (2013)
4 more