1UDC

STRUCTURE OF UDP-GALACTOSE-4-EPIMERASE COMPLEXED WITH UDP-MANNOSE

1UDC の概要

• エントリーDOI: 10.2210/pdb1udc/pdb
• 分子名称: UDP-GALACTOSE-4-EPIMERASE, SODIUM ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (7 entities in total)
• 機能のキーワード: udp-galactose, epimerase, isomerase
• 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: 38943.12

構造登録者

Thoden, J.B.,Holden, H.M. (登録日: 1997-01-06, 公開日: 1998-01-14, 最終更新日: 2024-02-14)

主引用文献

Thoden, J.B.,Hegeman, A.D.,Wesenberg, G.,Chapeau, M.C.,Frey, P.A.,Holden, H.M.
Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli.
Biochemistry, 36:6294-6304, 1997

PubMed Abstract: UDP-galactose 4-epimerase from Escherichia coli catalyzes the interconversion of UDP-galactose and UDP-glucose through the transient reduction of the tightly bound cofactor NAD+. The enzyme is unique among the NAD+-dependent enzymes in that it promotes stereospecific reduction of the cofactor but nonstereospecific hydride return during normal catalysis. In addition to hydride transfer, the reaction mechanism of epimerase involves two key features: the abstraction of a proton from the 4'-hydroxyl group of glucose or galactose by an active site base and the rotation of a 4-ketopyranose intermediate in the active site pocket. To address the second issue of movement within the active site, the X-ray structures of reduced epimerase complexed with UDP-mannose, UDP-4-deoxy-4-fluoro-alpha-D-galactose, or UDP-4-deoxy-4-fluoro-alpha-D-glucose have been determined and refined to 1.65, 1.8, and 1.65 A resolution, respectively. A comparison of these models to that of the previously determined epimerase/NADH/UDP-glucose abortive complex reveals that the active site accommodates the various sugars by simple rearrangements of water molecules rather than by large changes in side chain conformations. In fact, the polypeptide chains for all of the epimerase/NADH/UDP-sugar complexes studied thus far are remarkably similar and can be superimposed with root-mean-square deviations of not greater than 0.24 A. The only significant differences between the various enzyme/UDP-sugar models occur in two of the dihedral angles defining the conformation of the UDP-sugar ligands.

PubMed: 9174344
DOI: 10.1021/bi970025j

実験手法

X-RAY DIFFRACTION (1.65 Å)