› 1bsv

X-ray diffraction
2.2Å resolution

GDP-FUCOSE SYNTHETASE FROM ESCHERICHIA COLI COMPLEX WITH NADPH

Released:
DOI: 10.2210/pdb1bsv/pdb
Model geometry
Fit model/data
PDB entry 1bsv coloured by chain, front view.
PDB entry 1bsv coloured by chain, side view.
PDB entry 1bsv coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
GDP-fucose synthetase from Escherichia coli: structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site.
Somers WS, Stahl ML, Sullivan FX
Structure 6 1601-12 (1998)
PMID: 9862812

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: 36.19 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21
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

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 104.3Å b: 104.3Å c: 74.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 not available not available
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

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

4 mentions without citation

Structure and function of GDP-mannose-3',5'-epimerase: an enzyme which performs three chemical reactions at the same active site.
Major et al. (2005)
3 more