FIGURE 5.

Comparison of RNA-binding modules of negative-stranded RNA virus nucleoproteins. Electrostatic potential maps are shown for all proteins, with RNA depicted in stick form in cyan. The RNA-binding modules are shown in schematic diagrams above each eletrostatic potential map. Bases oriented to the top indicate that the bases face into protein, while bases oriented to the bottom suggest that the bases are exposed to solvent. (A) RVFV N, showing that only the N-terminal arm is available for N multimerization. The RNA-binding cleft hosts four ribonucleotides with all bases facing into the protein and three bases between two N subunits. (B) Rabies virus N. The N-terminal arm and the loop of the C-terminal domain are involved in mutimerization. The RNA-binding cleft of one protomer binds six ribonucleotides with bases 1, 2, 3, and 5 exposed to solvent, bases 4 and 6 facing into the protein, and three bases between protomers (bases 8 and 9 exposed to solvent and base 7 facing to the protein). (C) Vescular stomatitis virus N. The features of the multimerization and the RNA binding of the vescular stomatitis virus N is similar to that of the rabies virus with the bases 1, 2, 3, 4, 6, and 9 facing to solvent, and bases 5, 7, and 8 turning to protein. (D) N-terminal domain of Lassa fever virus nucleoprotein. The RNA-binding cleft binds six ribonucleotides, with all bases exposed to solvent.