Burnett R M, Grütter M G, White J L
J Mol Biol. 1985 Sep 5;185(1):105-23. doi: 10.1016/0022-2836(85)90186-x.
The structure of hexon, the major coat protein of 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. The main experimental finding derives from a low resolution electron density map calculated at 6.0 A resolution, but based on phases determined by the multiple isomorphous replacement method at 2.9 A resolution. Hexon consists of three subunits together forming two major components of different morphological symmetry. A triangular top with three towers of density is superimposed on a more bulky pseudo-hexagonal base. The symmetry of the top is in accord with the trimeric nature of hexon, but that of the base derives from the molecular function, which is to provide a densely packed impenetrable protective outer layer for the virion. A close-packed array of hexons forms a planar facet of the icosahedral capsid, with the tops presenting a spiky appearance that is consistent with electron micrographs of the adenovirus capsid. Hexon is hollow, permitting it to occupy a larger volume than normal for the same quantity of protein. The polypeptide chain has been traced in the 2.9 A electron density map for several non-contiguous stretches, allowing C alpha co-ordinates to be measured for 820 out of the 967 amino acid residues. The overall folding pattern confirms the assignment of shape, but the lack of connectivity so far precludes its complete description. The modest amount of alpha-helix and beta-sheet present is in accord with spectroscopic results.
