Fig. 5: Interaction between MARV L and VP35 tetramer. | Nature Communications

Fig. 5: Interaction between MARV L and VP35 tetramer.

From: Structural insights into the RNA-dependent RNA polymerase complexes from highly pathogenic Marburg and Ebola viruses

Fig. 5

a Surface representation of interaction between MARL and mVP35 tetramer. MARL is shown as molecular surfaces and colored by domains. mVP35 tetramer is shown by ribbons and colored by protomers. The interaction interfaces from d–i are indicated. b Different conformations of mVP35 protomers in the tetramer. The domains of mVP35 are indicated in the structures, including the oligomerization domain (OD), connection region (CR) and C-terminal domain (CTD) or interferon inhibitory domain (IID). c The interaction interface of MARL and VP35 tetramer are shown by surface electrostatic potentials, which were calculated by the APBS Electrostatics Plugin of PyMOL. The interaction interface is displayed in an open-book view. The approximate binding surface is outlined in yellow. d–i Detailed interactions between MARL and mVP35 from different regions as labeled in a. The main chains or side chains involved in hydrogen bonding, salt bridge, π–π stacking interactions and hydrophobic interactions are shown as sticks. Hydrogen bonds and salt bridges are shown by black dashed lines and the π–π stacking interactions is indicated by purple dashed lines.

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