› 1di0

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF LUMAZINE SYNTHASE FROM BRUCELLA ABORTUS

Released:
DOI: 10.2210/pdb1di0/pdb
PDB entry 1di0 coloured by chain, front view.
PDB entry 1di0 coloured by chain, side view.
PDB entry 1di0 coloured by chain, top view.
Source organism: Brucella abortus
Primary publication:
Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus.
Braden BC, Velikovsky CA, Cauerhff AA, Polikarpov I, Goldbaum FA
J Mol Biol 297 1031-6 (2000)
PMID: 10764570

Function and Biology Details

Reaction catalysed: 
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H(2)O + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo pentamer (preferred)
homo decamer
Assembly name:
PDBe Complex ID:
PDB-CPX-158311 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6,7-dimethyl-8-ribityllumazine synthase 2 Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 158 amino acids
Theoretical weight: 17.34 KDa
Source organism: Brucella abortus
Expression system: Escherichia coli
UniProt:
  • Canonical: P61711 (Residues: 1-158; Coverage: 100%)
Gene names: BruAb2_0535, ribH, ribH-2, ribH2
Sequence domains: 6,7-dimethyl-8-ribityllumazine synthase
Structure domains: Lumazine/riboflavin synthase

Ligands and Environments

1 bound ligand:
Ligand PO4 13 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: R32
Unit cell:
a: 142.25Å b: 142.25Å c: 242.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.23
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The origins and ongoing evolution of viruses.
Hendrix et al. (2000)
4 more

3 mentions without citation

The 2.2 A resolution structure of RpiB/AlsB from Escherichia coli illustrates a new approach to the ribose-5-phosphate isomerase reaction.
Zhang et al. (2003)
2 more