› 2hcv

X-ray diffraction
2Å resolution

Crystal structure of L-rhamnose isomerase from Pseudomonas stutzeri with metal ion

Released:
DOI: 10.2210/pdb2hcv/pdb
PDB entry 2hcv coloured by chain, front view.
PDB entry 2hcv coloured by chain, side view.
PDB entry 2hcv coloured by chain, top view.
Source organism: Pseudomonas stutzeri
Primary publication:
The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity.
Yoshida H, Yamada M, Ohyama Y, Takada G, Izumori K, Kamitori S
J Mol Biol 365 1505-16 (2007)
PMID: 17141803

Function and Biology Details

Reaction catalysed: 
L-rhamnopyranose = L-rhamnulose
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181127 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xylose isomerase-like TIM barrel domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 438 amino acids
Theoretical weight: 48 KDa
Source organism: Pseudomonas stutzeri
Expression system: Escherichia coli
UniProt:
  • Canonical: Q75WH8 (Residues: 1-430; Coverage: 100%)
Gene name: L-RhI
Sequence domains: Xylose isomerase-like TIM barrel
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

1 bound ligand:
Ligand ZN 8 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 74.257Å b: 103.972Å c: 107.023Å
α: 90° β: 106.81° γ: 90°
R-values:
R R work R free
0.155 0.155 0.192
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Isomerases for biotransformation of D-hexoses.
Mu et al. (2015)
1 more

2 mentions without citation

Structure of L-xylulose-5-Phosphate 3-epimerase (UlaE) from the anaerobic L-ascorbate utilization pathway of Escherichia coli: identification of a novel phosphate binding motif within a TIM barrel fold.
Shi et al. (2008)
1 more