› 3uzb

X-ray diffraction
3Å resolution

Crystal Structures of Branched-Chain Aminotransferase from Deinococcus radiodurans Complexes with alpha-Ketoisocaproate and L-Glutamate Suggest Its Radio-Resistance for Catalysis

Released:
DOI: 10.2210/pdb3uzb/pdb
PDB entry 3uzb coloured by chain, front view.
PDB entry 3uzb coloured by chain, side view.
PDB entry 3uzb coloured by chain, top view.
Source organism: Deinococcus radiodurans
Primary publication:
Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with α-ketoisocaproate and L-glutamate suggest the radiation resistance of this enzyme for catalysis.
Chen CD, Lin CH, Chuankhayan P, Huang YC, Hsieh YC, Huang TF, Guan HH, Liu MY, Chang WC, Chen CJ
J Bacteriol 194 6206-16 (2012)
PMID: 22984263

Function and Biology Details

Reaction catalysed: 
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193274 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Branched-chain-amino-acid aminotransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 358 amino acids
Theoretical weight: 39.47 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RTX5 (Residues: 1-358; Coverage: 100%)
Gene name: DR_1626
Sequence domains: Amino-transferase class IV
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
1 bound ligand:
Ligand COI 4 x COI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21
Unit cell:
a: 56.11Å b: 172.58Å c: 80.08Å
α: 90° β: 108.19° γ: 90°
R-values:
R R work R free
0.204 0.204 0.271
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Branched-Chain Amino Acids and Brain Metabolism.
Sperringer et al. (2017)
2 more

1 mention without citation

Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with α-ketoisocaproate and L-glutamate suggest the radiation resistance of this enzyme for catalysis.
Chen et al. (2012)