› 3xis

X-ray diffraction
1.6Å resolution

A METAL-MEDIATED HYDRIDE SHIFT MECHANISM FOR XYLOSE ISOMERASE BASED ON THE 1.6 ANGSTROMS STREPTOMYCES RUBIGINOSUS STRUCTURES WITH XYLITOL AND D-XYLOSE

Released:
DOI: 10.2210/pdb3xis/pdb
PDB entry 3xis coloured by chain, front view.
PDB entry 3xis coloured by chain, side view.
PDB entry 3xis coloured by chain, top view.
Source organism: Streptomyces rubiginosus
Primary publication:
A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 A Streptomyces rubiginosus structures with xylitol and D-xylose.
Whitlow M, Howard AJ, Finzel BC, Poulos TL, Winborne E, Gilliland GL
Proteins 9 153-73 (1991)
PMID: 2006134

Function and Biology Details

Reaction catalysed: 
Alpha-D-xylopyranose = alpha-D-xylufuranose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150204 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xylose isomerase Chain: A
Molecule details ›
Chain: A
Length: 387 amino acids
Theoretical weight: 43.15 KDa
Source organism: Streptomyces rubiginosus
Expression system: Not provided
UniProt:
  • Canonical: P24300 (Residues: 2-388; Coverage: 100%)
Gene name: xylA
Sequence domains: Xylose isomerase-like TIM barrel
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

3 bound ligands:
Ligand XYS 1 x XYS
Ligand XLS 1 x XLS
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 94.64Å b: 99.97Å c: 103.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
3 more

2 mentions without citation

Multiple structural alignment by secondary structures: algorithm and applications.
Dror et al. (2003)
1 more