› 1bws

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF GDP-4-KETO-6-DEOXY-D-MANNOSE EPIMERASE/REDUCTASE FROM ESCHERICHIA COLI A KEY ENZYME IN THE BIOSYNTHESIS OF GDP-L-FUCOSE

Released:
DOI: 10.2210/pdb1bws/pdb
PDB entry 1bws coloured by chain, front view.
PDB entry 1bws coloured by chain, side view.
PDB entry 1bws coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
GDP-4-keto-6-deoxy-D-mannose epimerase/reductase from Escherichia coli, a key enzyme in the biosynthesis of GDP-L-fucose, displays the structural characteristics of the RED protein homology superfamily.
Rizzi M, Tonetti M, Vigevani P, Sturla L, Bisso A, Flora AD, Bordo D, Bolognesi M
Structure 6 1453-65 (1998)
PMID: 9817848

Function and Biology Details

Reaction catalysed: 
GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152194 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GDP-L-fucose synthase Chain: A
Molecule details ›
Chain: A
Length: 321 amino acids
Theoretical weight: 36.17 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P32055 (Residues: 1-321; Coverage: 100%)
Gene names: JW2037, b2052, fcl, wcaG, yefB
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 1 x NDP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 104.2Å b: 104.2Å c: 75.88Å
α: 90° β: 90° γ: 120°
Expression system: Escherichia coli

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Citations

4 review citations

Fucose: biosynthesis and biological function in mammals.
Becker et al. (2003)
3 more

2 mentions without citation

Predicting protein function from structure--the roles of short-chain dehydrogenase/reductase enzymes in Bordetella O-antigen biosynthesis.
King et al. (2007)
1 more