› 3v0u

X-ray diffraction
2.2Å resolution

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

Released:
DOI: 10.2210/pdb3v0u/pdb
PDB entry 3v0u coloured by chain, front view.
PDB entry 3v0u coloured by chain, side view.
PDB entry 3v0u 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

Assemblies composition:
monomeric (preferred)
homo dimer
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: 338 amino acids
Theoretical weight: 37.46 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 58.102Å b: 93.65Å c: 143.077Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.212 0.247
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