› 4tsk

X-ray diffraction
2.5Å resolution

Ketol-acid reductoisomerase from Alicyclobacillus acidocaldarius

Released:
DOI: 10.2210/pdb4tsk/pdb
PDB entry 4tsk coloured by chain, front view.
PDB entry 4tsk coloured by chain, side view.
PDB entry 4tsk coloured by chain, top view.
Source organism: Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446
Primary publication:
Uncovering rare NADH-preferring ketol-acid reductoisomerases.
Brinkmann-Chen S, Cahn JKB, Arnold FH
Metab Eng 26 17-22 (2014)
PMID: 25172159

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111822 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ketol-acid reductoisomerase (NADP(+)) Chain: A
Molecule details ›
Chain: A
Length: 350 amino acids
Theoretical weight: 38.79 KDa
Source organism: Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: C8WR67 (Residues: 1-344; Coverage: 100%)
Gene names: Aaci_2227, ilvC
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 1 x NDP
2 bound ligands:
Ligand MG 3 x MG
Ligand TLA 1 x TLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P23
Unit cell:
a: 124.099Å b: 124.099Å c: 124.099Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.154 0.182
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Protein Engineering for Nicotinamide Coenzyme Specificity in Oxidoreductases: Attempts and Challenges.
Chánique et al. (2018)
1 more

3 mentions without citation

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