1BWS

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

Summary for 1BWS

• Entry DOI: 10.2210/pdb1bws/pdb
• Descriptor: PROTEIN (GDP-4-KETO-6-DEOXY-D-MANNOSE EPIMERASE/REDUCTASE), NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: epimerase/reductase, gdp-l-fucose biosynthesis, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 36918.50

Authors

Rizzi, M.,Tonetti, M.,Flora, A.D.,Bolognesi, M. (deposition date: 1998-09-25, release date: 1999-01-13, Last modification date: 2024-02-07)

Primary citation

Rizzi, M.,Tonetti, M.,Vigevani, P.,Sturla, L.,Bisso, A.,Flora, A.D.,Bordo, D.,Bolognesi, M.
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.
Structure, 6:1453-1465, 1998

PubMed Abstract: The process of guanosine 5'-diphosphate L-fucose (GDP-L-fucose) biosynthesis is conserved throughout evolution from prokaryotes to man. In animals, GDP-L-fucose is the substrate of fucosyltransferases that participate in the biosynthesis and remodeling of glycoconjugates, including ABH blood group and Lewis-system antigens. The 'de novo' pathway of GDP-L-fucose biosynthesis from GDP-D-mannose involves a GDP-D-mannose 4,6 dehydratase (GMD) and a GDP-4-keto-6-deoxy-D-mannose epimerase/reductase (GMER). Neither of the catalytic mechanisms nor the three-dimensional structures of the two enzymes has been elucidated yet. The severe leukocyte adhesion deficiency (LAD) type II genetic syndrome is known to result from deficiencies in this de novo pathway.

PubMed: 9817848
DOI: 10.1016/S0969-2126(98)00144-0

Experimental method

X-RAY DIFFRACTION (2.2 Å)