› 4gji

X-ray diffraction
1.7Å resolution

Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant H101N in complex with L-rhamnopyranose

Released:
DOI: 10.2210/pdb4gji/pdb
PDB entry 4gji coloured by chain, front view.
PDB entry 4gji coloured by chain, side view.
PDB entry 4gji coloured by chain, top view.
Source organism: Pseudomonas stutzeri
Primary publication:
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 H, Yoshihara A, Teraoka M, Yamashita S, Izumori K, Kamitori S
FEBS Open Bio 3 35-40 (2013)
PMID: 23772372

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: 47.98 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

4 bound ligands:
Ligand RNS 4 x RNS
Ligand RAM 4 x RAM
Ligand MN 10 x MN
Ligand RM4 3 x RM4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P21
Unit cell:
a: 75.124Å b: 104.917Å c: 112.376Å
α: 90° β: 106.01° γ: 90°
R-values:
R R work R free
0.177 0.175 0.195
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Regulation of the rhaEWRBMA Operon Involved in l-Rhamnose Catabolism through Two Transcriptional Factors, RhaR and CcpA, in Bacillus subtilis.
Hirooka et al. (2015)
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)