› 1yve

X-ray diffraction
1.65Å resolution

ACETOHYDROXY ACID ISOMEROREDUCTASE COMPLEXED WITH NADPH, MAGNESIUM AND INHIBITOR IPOHA (N-HYDROXY-N-ISOPROPYLOXAMATE)

Released:
DOI: 10.2210/pdb1yve/pdb
PDB entry 1yve coloured by chain, front view.
PDB entry 1yve coloured by chain, side view.
PDB entry 1yve coloured by chain, top view.
Source organism: Spinacia oleracea
Primary publication:
The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution.
Biou V, Dumas R, Cohen-Addad C, Douce R, Job D, Pebay-Peyroula E
EMBO J 16 3405-15 (1997)
PMID: 9218783

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:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169546 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ketol-acid reductoisomerase, chloroplastic Chains: I, J, K, L
Molecule details ›
Chains: I, J, K, L
Length: 524 amino acids
Theoretical weight: 57.05 KDa
Source organism: Spinacia oleracea
Expression system: Escherichia coli
UniProt:
  • Canonical: Q01292 (Residues: 72-595; Coverage: 88%)
Gene name: AHRI
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 4 x NDP
3 bound ligands:
Ligand MG 8 x MG
Ligand CL 3 x CL
Ligand HIO 4 x HIO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 111.43Å b: 61.94Å c: 162.54Å
α: 90° β: 95.08° γ: 90°
R-values:
R R work R free
0.197 0.197 0.239
Expression system: Escherichia coli

Quick links

Citations

7 review citations

The aspartic acid metabolic pathway, an exciting and essential pathway in plants.
Azevedo et al. (2006)
6 more

15 mentions without citation

Knotted proteins: A tangled tale of Structural Biology.
Faísca PF. (2015)
14 more