› 3itl

X-ray diffraction
1.7Å resolution

Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant D327N in complex with L-rhamnulose

Released:
DOI: 10.2210/pdb3itl/pdb
PDB entry 3itl coloured by chain, front view.
PDB entry 3itl coloured by chain, side view.
PDB entry 3itl coloured by chain, top view.
Source organism: Pseudomonas stutzeri
Primary publication:
Catalytic reaction mechanism of Pseudomonas stutzeri L-rhamnose isomerase deduced from X-ray structures.
Yoshida H, Yamaji M, Ishii T, Izumori K, Kamitori S
FEBS J 277 1045-57 (2010)
PMID: 20088877

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

2 bound ligands:
Ligand MN 8 x MN
Ligand LRH 4 x LRH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 74.7Å b: 104.634Å c: 115.096Å
α: 90° β: 108.14° γ: 90°
R-values:
R R work R free
0.167 0.165 0.188
Expression system: Escherichia coli

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Citations

2 review citations

Enzymatic approaches to rare sugar production.
Zhang et al. (2017)
1 more

1 mention without citation

Structure of l-rhamnose isomerase in complex with l-rhamnopyranose demonstrates the sugar-ring opening mechanism and the role of a substrate sub-binding site.
Yoshida et al. (2013)