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

1BWS の概要

• エントリーDOI: 10.2210/pdb1bws/pdb
• 分子名称: PROTEIN (GDP-4-KETO-6-DEOXY-D-MANNOSE EPIMERASE/REDUCTASE), NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: epimerase/reductase, gdp-l-fucose biosynthesis, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36918.50

構造登録者

Rizzi, M.,Tonetti, M.,Flora, A.D.,Bolognesi, M. (登録日: 1998-09-25, 公開日: 1999-01-13, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)