› 2qcx

X-ray diffraction
2.2Å resolution

Crystal structure of Bacillus subtilis TenA Y112F mutant complexed with formyl aminomethyl pyrimidine

Released:
DOI: 10.2210/pdb2qcx/pdb
Model geometry
Fit model/data
PDB entry 2qcx coloured by chain, front view.
PDB entry 2qcx coloured by chain, side view.
PDB entry 2qcx coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis.
Jenkins AL, Zhang Y, Ealick SE, Begley TP
Bioorg Chem 36 29-32 (2008)
PMID: 18054064

Function and Biology Details

Reaction catalysed: 
4-amino-5-aminomethyl-2-methylpyrimidine + H(2)O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + ammonia
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150337 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminopyrimidine aminohydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 30.55 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P25052 (Residues: 1-236; Coverage: 100%)
Gene names: BSU11650, tenA
Sequence domains: TENA/THI-4/PQQC family
Structure domains: Heme oxygenase-like

Ligands and Environments

1 bound ligand:
Ligand PF1 2 x PF1
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P41212
Unit cell:
a: 58.625Å b: 58.625Å c: 296.469Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.233
Expression system: Escherichia coli

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Citations

3 review citations

The structural and biochemical foundations of thiamin biosynthesis.
Jurgenson et al. (2009)
2 more

1 mention without citation

In silico analysis of heme oxygenase structural homologues identifies group-specific conservations.
Irvin et al. (2017)