› 6azo

X-ray diffraction
2.46Å resolution

Structural and biochemical characterization of a non-canonical biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841

Released:
DOI: 10.2210/pdb6azo/pdb
PDB entry 6azo coloured by chain, front view.
PDB entry 6azo coloured by chain, side view.
PDB entry 6azo coloured by chain, top view.
Source organism: Rhizobium leguminosarum bv. viciae 3841
Primary publication:
Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841.
Esquirol L, Peat TS, Wilding M, Lucent D, French NG, Hartley CJ, Newman J, Scott C
OpenAccess logo PLoS One 13 e0192736 (2018)
PMID: 29425231

Function and Biology Details

Reaction catalysed: 
Biuret + H(2)O = urea-1-carboxylate + NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172972 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biuret amidohydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 262 amino acids
Theoretical weight: 29.07 KDa
Source organism: Rhizobium leguminosarum bv. viciae 3841
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q1M7F4 (Residues: 1-233; Coverage: 100%)
Gene names: biuH, pRL100352
Sequence domains: Isochorismatase family

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
1 modified residue:
Ligand MSE 36 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: C2
Unit cell:
a: 135.688Å b: 100.957Å c: 65.605Å
α: 90° β: 91.84° γ: 90°
R-values:
R R work R free
0.228 0.225 0.276
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme.
Esquirol et al. (2018)
5 more

4 mentions without citation

Using photons to manipulate enzyme inhibition by an azobenzene-modified nucleic acid probe.
Kim et al. (2009)
3 more