› 2hxu

X-ray diffraction
1.8Å resolution

Crystal structure of K220A mutant of L-Fuconate Dehydratase from Xanthomonas campestris liganded with Mg++ and L-fuconate

Released:
DOI: 10.2210/pdb2hxu/pdb
PDB entry 2hxu coloured by chain, front view.
PDB entry 2hxu coloured by chain, side view.
PDB entry 2hxu coloured by chain, top view.
Source organism: Xanthomonas campestris pv. campestris
Primary publication:
Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris.
Yew WS, Fedorov AA, Fedorov EV, Rakus JF, Pierce RW, Almo SC, Gerlt JA
Biochemistry 45 14582-97 (2006)
PMID: 17144652

Function and Biology Details

Reaction catalysed: 
L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-fuconate dehydratase Chain: A
Molecule details ›
Chain: A
Length: 441 amino acids
Theoretical weight: 48.12 KDa
Source organism: Xanthomonas campestris pv. campestris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8P3K2 (Residues: 1-441; Coverage: 100%)
Gene name: XCC4069
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand SO4 3 x SO4
Ligand LFC 1 x LFC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P622
Unit cell:
a: 159.154Å b: 159.154Å c: 101.961Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.172 0.183
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Divergent evolution in enolase superfamily: strategies for assigning functions.
Gerlt et al. (2012)
3 more