1BSV
GDP-FUCOSE SYNTHETASE FROM ESCHERICHIA COLI COMPLEX WITH NADPH
Summary for 1BSV
| Entry DOI | 10.2210/pdb1bsv/pdb |
| Descriptor | PROTEIN (GDP-FUCOSE SYNTHETASE), NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | epimerase-reductase, nadph, gdp-fucose, oxidoreductase |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P32055 |
| Total number of polymer chains | 1 |
| Total formula weight | 36932.52 |
| Authors | Somers, W.S.,Stahl, M.L.,Sullivan, F.X. (deposition date: 1998-08-31, release date: 1999-08-26, Last modification date: 2023-08-09) |
| Primary citation | Somers, W.S.,Stahl, M.L.,Sullivan, F.X. 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. Structure, 6:1601-1612, 1998 Cited by PubMed Abstract: . In all species examined, GDP-fucose is synthesized from GDP-mannose in a three-step reaction catalyzed by two enzymes, GDP-mannose 4,6 dehydratase and a dual function 3, 5-epimerase-4-reductase named GDP-fucose synthetase. In this latter aspect fucose biosynthesis differs from that of other deoxy and dideoxy sugars, in which the epimerase and reductase activities are present as separate enzymes. Defects in GDP-fucose biosynthesis have been shown to affect nodulation in bacteria, stem development in plants, and are associated with the immune defect leukocyte adhesion deficiency type II in humans. PubMed: 9862812DOI: 10.1016/S0969-2126(98)00157-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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