Fig. 4: Formation of σNS filaments. | Nature Communications

Fig. 4: Formation of σNS filaments.

From: Structure of orthoreovirus RNA chaperone σNS, a component of viral replication factories

Fig. 4

a Surface representation of the helical assembly formed by σNS dimers using crystallographic P65 symmetry along the crystallographic c axis. Dimers are depicted as blue and green subunits. A single helical turn (80 Å in length) is demarcated in the purple-dotted frame. b A 90o rotation around the horizontal axis perpendicular to the filament shows the central tunnel. The tunnel is 40 Å in width, and the total diameter of the filament is 150 Å. c Single helical turn formed by six σNS dimers. Dimers are depicted in different colors. One pair of interacting dimers (pink and cyan) are demarcated in a yellow frame. The location of the N-terminal arm of the pink dimer interacting with the cyan dimer is shown within the red frame. d Interacting dimers (pink and blue, two monomeric subunits in the pink dimer denoted A and A') corresponding to the yellow frame in c are shown separately to illustrate how the N-terminal arms (in red frame) project away in opposite directions (thick red arrows) to chain-link the neighboring dimers to form the helical assembly shown in Fig. 4a. e Ligplot of interactions between N-terminal arm residues of the pink dimer and core domain residues of the blue dimer. Residues involved in hydrophobic interactions are shown by brick-red and pink spoked arcs, and hydrogen bond interactions between the residues are indicated by green lines, with carbon, oxygen, and nitrogen atoms depicted in black, red, and blue, respectively. Note the involvement of the Se-Met residue at position 1 (Mse 1), indicated by an asterisk.

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