› 4xdy

X-ray diffraction
1.54Å resolution

Structure of NADH-preferring ketol-acid reductoisomerase from an uncultured archean

Released:
DOI: 10.2210/pdb4xdy/pdb
PDB entry 4xdy coloured by chain, front view.
PDB entry 4xdy coloured by chain, side view.
PDB entry 4xdy coloured by chain, top view.
Source organism: uncultured archaeon GZfos26G2
Primary publication:
Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases.
Cahn JK, Brinkmann-Chen S, Spatzal T, Wiig JA, Buller AR, Einsle O, Hu Y, Ribbe MW, Arnold FH
Biochem J 468 475-84 (2015)
PMID: 25849365

Function and Biology Details

Reaction catalysed: 
(2R)-2,3-dihydroxy-3-methylbutanoate + NAD(+) = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179161 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ketol-acid reductoisomerase (NAD(+)) Chains: A, B
Molecule details ›
Chains: A, B
Length: 338 amino acids
Theoretical weight: 37.73 KDa
Source organism: uncultured archaeon GZfos26G2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q64BR7 (Residues: 1-332; Coverage: 100%)
Gene names: GZ26G2_30, ilvC
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAI 2 x NAI
3 bound ligands:
Ligand MG 6 x MG
Ligand GOL 2 x GOL
Ligand HIO 2 x HIO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Unit cell:
a: 49.695Å b: 141.748Å c: 148.598Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.209
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Bacterial Branched-Chain Amino Acid Biosynthesis: Structures, Mechanisms, and Drugability.
Amorim Franco et al. (2017)
8 other articles

2 mentions without citation

A General Tool for Engineering the NAD/NADP Cofactor Preference of Oxidoreductases.
Cahn et al. (2017)
1 more