Fig. 2: Structures of the C14 anchor complexes from the apical cap and basal structure. | Nature Communications

Fig. 2: Structures of the C14 anchor complexes from the apical cap and basal structure.

From: Structure of AcMNPV nucleocapsid reveals DNA portal organization and packaging apparatus of circular dsDNA baculovirus

Fig. 2

A, B 3D reconstructions of the anchor-1/anchor-2 complex of the apical cap and basal structure, respectively, colored by protein composition (color key below). C, D Ribbon representation of the proteins composing the asymmetric unit of the apical and basal anchor-1/anchor-2 respectively colored as in (A). The dotted line in (C) delineates the anchor-2 complex. E Detailed view of the region highlighted in (D), showing two consecutive asymmetric units (aui and aui+1). Two key interactions are observed: VP39_1 from anchor-1 of aui interacts with the Ac144/Ac101 module of aui+1. Similarly, VP39_2 from anchor-1 of aui interacts with the Ac144/Ac101 module of the same asymmetric unit. F Detailed view of the region highlighted in (D), showing VP39_4 N terminus from anchor-1 of aui interacting with Ac98 from anchor-2 of aui and the lower Ac144/Ac101 module of anchor-2 from aui-1. Predicted hydrogen bond-forming residues include: M8 for VP39_4, L32 and Y40 for Ac98 and, D273 and N279 for Ac102. G Zoomed view of the interaction region highlighted in (E), where residues 264 to 276 of VP39_1 of anchor-1 of aui engage with residues 259 to 273 of Ac101 and the C-terminus of Ac142 of aui+1. Predicted hydrogen bond-forming residues include: N264, R265, L266, L272, K273 for Vp39_1, Q261, Y262, T267, E268, I 269, F271 for Ac101 and Q406 for Ac142. H Zoomed view of the interaction region highlighted in (E). The N-terminus of vp39_2 of anchor-1 of aui interacts with both Ac144 and Ac101 of anchor-2 of the same asymmetric unit. Hydrogen bond-forming residues include: L3, Q12, R14 for Vp39_2, E276, R280 for Ac102 and S59, M63, Q65, S200 for Ac144. I Close-up of the region highlighted in (C) showing the interaction of PTP (pink) with Ac142 (yellow) and an Ac66 dimer (purple and magenta). Predicted hydrogen bond-forming residues are: PTP/Ac142 interaction: H7, N8, Y35, T37, E40 for PTP and N180, P209, K225, K216, N218, S220 for Ac142. PTP/Ac66 interaction: K109, P111, M113 for PTP, Q315, R322 for Ac66_1 and Q317 for Ac66_2).

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