› 4rhl

X-ray diffraction
3.1Å resolution

Crystal structure of T. brucei arginase-like protein triple mutant S149D/R151H/S226D bound with Mn2+

Released:
DOI: 10.2210/pdb4rhl/pdb
PDB entry 4rhl coloured by chain, front view.
PDB entry 4rhl coloured by chain, side view.
PDB entry 4rhl coloured by chain, top view.
Source organism: Trypanosoma brucei brucei TREU927
Primary publication:
Crystal structure of an arginase-like protein from Trypanosoma brucei that evolved without a binuclear manganese cluster.
Hai Y, Kerkhoven EJ, Barrett MP, Christianson DW
OpenAccess logo Biochemistry 54 458-71 (2015)
PMID: 25536859

Function and Biology Details

Reaction catalysed: 
L-arginine + H(2)O = L-ornithine + urea
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-560864 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase, putative Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 38.77 KDa
Source organism: Trypanosoma brucei brucei TREU927
Expression system: Escherichia coli
UniProt:
  • Canonical: Q581Y0 (Residues: 1-331; Coverage: 100%)
Gene names: Tb08.26N11.490, Tb927.8.2020
Sequence domains: Arginase family
Structure domains: Ureohydrolase domain

Ligands and Environments

2 bound ligands:
Ligand MN 2 x MN
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P321
Unit cell:
a: 135.582Å b: 135.582Å c: 86.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.215 0.274
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Comparative Metabolism of Free-living Bodo saltans and Parasitic Trypanosomatids.
Opperdoes et al. (2016)
5 more

1 mention without citation

Crystal structure of an arginase-like protein from Trypanosoma brucei that evolved without a binuclear manganese cluster.
Hai et al. (2015)