› 3v0s

X-ray diffraction
1.77Å resolution

Crystal Structure of Perakine Reductase, Founder Member of a Novel AKR Subfamily with Unique Conformational Changes during NADPH Binding

Released:
DOI: 10.2210/pdb3v0s/pdb
PDB entry 3v0s coloured by chain, front view.
PDB entry 3v0s coloured by chain, side view.
PDB entry 3v0s coloured by chain, top view.
Source organism: Rauvolfia serpentina
Primary publication:
Crystal structure of perakine reductase, founding member of a novel aldo-keto reductase (AKR) subfamily that undergoes unique conformational changes during NADPH binding.
Sun L, Chen Y, Rajendran C, Mueller U, Panjikar S, Wang M, Mindnich R, Rosenthal C, Penning TM, Stöckigt J
J Biol Chem 287 11213-21 (2012)
PMID: 22334702

Function and Biology Details

Reaction catalysed: 
Raucaffrinoline + NADP(+) = perakine + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Perakine reductase Chain: A
Molecule details ›
Chain: A
Length: 337 amino acids
Theoretical weight: 37.47 KDa
Source organism: Rauvolfia serpentina
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3L181 (Residues: 1-337; Coverage: 100%)
Gene name: PR
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

1 bound ligand:
Ligand ATR 1 x ATR
3 modified residues:
Ligand MLZ 3 x MLZ
Ligand M3L 2 x M3L
Ligand MLY 1 x MLY

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3221
Unit cell:
a: 55.199Å b: 55.199Å c: 210.228Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.184 0.212
Expression system: Escherichia coli

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Citations

2 review citations

Plant aldo-keto reductases (AKRs) as multi-tasking soldiers involved in diverse plant metabolic processes and stress defense: A structure-function update.
Sengupta et al. (2015)
1 more

1 mention without citation

Crystal structure of perakine reductase, founding member of a novel aldo-keto reductase (AKR) subfamily that undergoes unique conformational changes during NADPH binding.
Sun et al. (2012)