Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution.
An atomic model of the tetrameric surface glycoprotein neuraminidase of influenza virus A/Tokyo/3/67 has been built and refined based on X-ray diffraction data at 2.2 A resolution. The crystallographic residual is 0.21 for data between 6 and 2.2 A resolution and the r.m.s. deviations from ideal geometry are 0.02 A for bond lengths and 3.9 degrees for bond angles. The model includes amino acid residues 83 to 469, four oligosaccharide structures N-linked at asparagine residues 86, 146, 200 and 234, a single putative Ca2+ ion site, and 85 water molecules. One of the oligosaccharides participates in a novel crystal contact. The folding pattern is a beta-sheet propeller as described earlier and details of the intramolecular interactions between the six beta-sheets are presented. Strain-invariant residues are clustered around the propeller axis on the upper surface of the molecule where they line the wall of a cavity into which sialic has been observed to bind. Strain-variable residues implicated in binding to antibodies surround this site.
Varghese
J N
JN
CSIRO Division of Biomolecular Engineering, Parkville, Victoria, Australia.
Colman
P M
PM
D000940:Antigenic Variation; D006031:Glycosylation; D006860:Hydrogen Bonding; D009980:Influenza A virus / Q000201:enzymology* / Q000276:immunology; D008670:Metals / Q000737:chemistry; D009439:Neuraminidase / Q000737:chemistry* / Q000276:immunology; D009844:Oligosaccharides / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D013045:Species Specificity; D013379:Substrate Specificity; D014961:X-Ray Diffraction
D008670:Metals; D009844:Oligosaccharides; D010455:Peptides; D009439:Neuraminidase