The molecular structure and structural transition of the α-helical capsid in filamentous bacteriophage Pf1

Welsh, L.C.; Symmons, M.F.; Marvin, D.A.

doi:10.1107/S0907444999015334

Figure 8
Grouping of subunits in the perturbed helix. Views perpendicular to the virion axis, N-termini of the subunits towards the top. Colour coding as in Fig. 6

. (a) Units k = 1 and k = 2 in the virion basic helix are superposed on unit k = 0 by the operation (−kT^H, −kH^H). Black, model ^RPf1^H; red, unit k = 0 of model ^3RPf1^H; green, k = 1; blue, k = 2. Heavy lines connect C^α atoms; lighter lines connect side-chain non-H atoms. Stereoview from outside the virion towards the virion axis, which is shown as a vertical line. (b) Models as (a) but viewed at 90° to (a), tangent to the circumference of a cylinder coaxial with the virion, in the direction of increasing cylindrical polar angle φ. (c) The assembly of subunits in model ^3RPf1^H. Each subunit is represented as a space-filling coil following the protein backbone at 5 Å radius. Axial slab about 100 Å long, corresponding to about 0.5% of the total length of the virion. Colour coding as in (a): red, k = 0, 3, 6, 9, …; green, k = 1, 4, 7, 10, …; blue, k = 2, 5, 8, 11, … . Three adjacent subunits (k = 0, −6, −11) are shown in atomic detail (white lines) within `transparent' rods. Heavy lines connect C^α atoms; lighter lines connect side-chain non-H atoms.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 56| Part 2| February 2000| Pages 137-150

doi:10.1107/S0907444999015334

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