2NZX

Crystal Structure of alpha1,3-Fucosyltransferase with GDP

Summary for 2NZX

• Entry DOI: 10.2210/pdb2nzx/pdb
• Related: 2NZW 2NZY
• Descriptor: Alpha1,3-fucosyltransferase, GUANOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: alpha1, 3-fucosyltransferase, fucosyltransferase, fuct, gt 10, transferase
• Biological source: Helicobacter pylori
• Cellular location: Membrane ; Peripheral membrane protein : O30511
• Total number of polymer chains: 3
• Total formula weight: 130795.74

Authors

Sun, H.Y.,Ko, T.P. (deposition date: 2006-11-27, release date: 2007-01-23, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)