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. Author manuscript; available in PMC: 2014 Sep 2.
Published in final edited form as: Nature. 2000 Dec 7;408(6813):745–750. doi: 10.1038/35047129

Figure 2.

Figure 2

Connector structure ribbon diagrams. a, The dodecameric connector seen from the tail looking towards the head; b, a side view with the pRNA-binding site at the bottom, showing the conical structure of the connector and the helical twist of each subunit around the 12-fold axis (white); c, a stereo diagram of a pair of monomers. One monomer is coloured red in the central domain, green in the wide-end domain that resides inside the capsid, and yellow at the narrow-end domain. The other monomers are all coloured blue. The ordered part of the polypeptide starts with helix α1 on the outside of the connector, going towards the wide end (residues 61 to 128 and 247 to 286). Helix α3 (residues 129 to 157) returns the chain to the narrow end (residues 158 to 202). The tip of the connector at the narrow end is formed by residues 164 to 170 and 185 to 196. Helix α5 (residues 208 to 226) returns the polypeptide to the wide end through the second disordered section. (Drawn with the program MOLSCRIPT25 and RASTER3D25.)