NEW TRIPLE-HELICAL MODEL FOR THE SHAFT OF THE ADENOVIRUS FIBER

The adenovirus fibre is a trimeric protein with a globular head on a long thin shaft that projects from the twelve fivefold vertices of the virion. The shaft region of the fibre primary sequence has a unique pseudo-repeating motif of 15 residues. Using constraints derived from sequence analysis, the trimeric nature of the fibre, the experimental determination of the shaft length and general knowledge about protein structure, an atomic model of the fibre shaft has been constructed by computer modelling techniques. In the final model the three monomers form a left-handed triple-helical structure with threefold symmetry and with successive 15-residue repeats on the same chain related by an axial of 13·1 Å and a left-handed azimuthal rotation of close to 300°. Three threefold related β-sheets with short strands are formed by inter-monomer main-chain hydrogen bonds giving rise to superhelical ribbons covering the surface of the shaft. The model satisfies criteria of extensive hydrogen bonding, reasonable backbone torsion angles, burial of most hydrophobic resedues and good packing of the hydrophobic core. Furthermore,the model is consistent with the observed shaft length of about 290 Å and its calculated X-ray fibre diffraction pattern shows the characteristic features found in the diffraction pattern of crystals of fibre, notably layer lines with a spacing of about 1 26 Å-1 and strong meridional intensity at 1 44 Å1 ̄. © 1992.