2NZY

Crystal Structure of alpha1,3-Fucosyltransferase with GDP-fucose

2NZY の概要

• エントリーDOI: 10.2210/pdb2nzy/pdb
• 関連するPDBエントリー: 2NZW 2NZX
• 分子名称: Alpha1,3-Fucosyltransferase, alpha-L-fucopyranose, GUANOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: alpha1, 3-fucosyltransferase, fucosyltransferase, fuct, gt 10, transferase
• 由来する生物種: Helicobacter pylori
• 細胞内の位置: Membrane ; Peripheral membrane protein : O30511
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 131384.27

構造登録者

Sun, H.Y.,Ko, T.P. (登録日: 2006-11-27, 公開日: 2007-01-23, 最終更新日: 2023-10-25)

主引用文献

Sun, H.Y.,Lin, S.W.,Ko, T.P.,Pan, J.F.,Liu, C.L.,Lin, C.N.,Wang, A.H.,Lin, C.H.
Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design.
J. Biol. Chem., 282:9973-9982, 2007

PubMed Abstract: Helicobacter pylori alpha1,3-fucosyltransferase (FucT) is involved in catalysis to produce the Lewis x trisaccharide, the major component of the bacteria's lipopolysaccharides, which has been suggested to mimic the surface sugars in gastric epithelium to escape host immune surveillance. We report here three x-ray crystal structures of FucT, including the FucT.GDP-fucose and FucT.GDP complexes. The protein structure is typical of the glycosyltransferase-B family despite little sequence homology. We identified a number of catalytically important residues, including Glu-95, which serves as the general base, and Glu-249, which stabilizes the developing oxonium ion during catalysis. The residues Arg-195, Tyr-246, Glu-249, and Lys-250 serve to interact with the donor substrate, GDP-fucose. Variations in the protein and ligand conformations, as well as a possible FucT dimer, were also observed. We propose a catalytic mechanism and a model of polysaccharide binding not only to explain the observed variations in H. pylori lipopolysaccharides, but also to facilitate the development of potent inhibitors.

PubMed: 17251184
DOI: 10.1074/jbc.M610285200

実験手法

X-RAY DIFFRACTION (2.05 Å)