The structure of the adenovirus capsid: I. An envelope model of hexon at 6 Å resolution

摘要: Abstract The structure of hexon, the major coat protein adenovirus, has been determined by X-ray crystallography. Electron density maps were obtained with phases based on five heavy-atom derivatives at 2.9 A resolution. main experimental finding derives from a low resolution electron map calculated 6.0 resolution, but multiple isomorphous replacement method Hexon consists three subunits together forming two components different morphological symmetry. triangular top towers is superimposed more bulky pseudo-hexagonal base. symmetry in accord trimeric nature that base molecular function, which to provide densely packed impenetrable protective outer layer for virion. closepacked array hexons forms planar facet icosahedral capsid, tops presenting spiky appearance consistent micrographs adenovirus capsid. hollow, permitting it occupy larger volume than normal same quantity protein. polypeptide chain traced several non-contiguous stretches, allowing C α co-ordinates be measured 820 out 967 amino acid residues. overall folding pattern confirms assignment shape, lack connectivity so far precludes its complete description. modest amount α-helix and β-sheet present spectroscopic results.