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X-ray diffraction
2.82Å resolution

THE CRYSTAL STRUCTURE OF UMP KINASE FROM BACILLUS ANTHRACIS (BA1797)

Released:
DOI: 10.2210/pdb2jjx/pdb
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Source organism: Bacillus anthracis str. Ames
Primary publication:
The crystal structure of UMP kinase from Bacillus anthracis (BA1797) reveals an allosteric nucleotide-binding site.
Meier C, Carter LG, Sainsbury S, Mancini EJ, Owens RJ, Stuart DI, Esnouf RM
J Mol Biol 381 1098-105 (2008)
PMID: 18625239

Function and Biology Details

Reaction catalysed: 
UMP + ATP = UDP + ADP.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-105704 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridylate kinase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 255 amino acids
Theoretical weight: 28.33 KDa
Source organism: Bacillus anthracis str. Ames
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A6L7HKK4 (Residues: 1-247; Coverage: 100%)
Gene names: GBAA_1797, pyrH, pyrH1
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

2 bound ligands:
Ligand ATP 3 x ATP
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P6122
Unit cell:
a: 87.3Å b: 87.3Å c: 383.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.2 0.252
Expression system: Escherichia coli

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Citations

9 citation in other articles

Role of purine biosynthesis in Bacillus anthracis pathogenesis and virulence.
Jenkins et al. (2011)
8 more

4 mentions without citation

The structural basis of ATP as an allosteric modulator.
Lu et al. (2014)
3 more

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