› 1ye4

X-ray diffraction
2.4Å resolution

Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+

Released:
DOI: 10.2210/pdb1ye4/pdb
PDB entry 1ye4 coloured by chain, front view.
PDB entry 1ye4 coloured by chain, side view.
PDB entry 1ye4 coloured by chain, top view.
Source organism: Yamadazyma tenuis
Primary publication:
Fine tuning of coenzyme specificity in family 2 aldo-keto reductases revealed by crystal structures of the Lys-274-->Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+ and NADP+.
Leitgeb S, Petschacher B, Wilson DK, Nidetzky B
FEBS Lett 579 763-7 (2005)
PMID: 15670843

Function and Biology Details

Reaction catalysed: 
Xylitol + NAD(P)(+) = D-xylose + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-130775 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(P)H-dependent D-xylose reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 322 amino acids
Theoretical weight: 36.09 KDa
Source organism: Yamadazyma tenuis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O74237 (Residues: 1-322; Coverage: 100%)
Gene names: XYL1, XYLR
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
1 bound ligand:
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: C2
Unit cell:
a: 182.827Å b: 128.666Å c: 80.101Å
α: 90° β: 90.11° γ: 90°
R-values:
R R work R free
0.206 0.206 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Ethanol production from xylose in engineered Saccharomyces cerevisiae strains: current state and perspectives.
Matsushika et al. (2009)
4 more

1 mention without citation

Identification of a novel NADH-specific aldo-keto reductase using sequence and structural homologies.
Di Luccio et al. (2006)