Fig. 1: Overview of the map and model of MARV L–VP35 complex. | Nature Communications

Fig. 1: Overview of the map and model of MARV L–VP35 complex.

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

Fig. 1

a Orthogonal view of the cryo-EM map of MARV L–VP35 complex. Visible domains in the map of MARL including the RNA-dependent RNA polymerase (RdRp) domain and the polyribonucleotidyl transferase (PRNTase or capping) domain as well as four mVP35 protomers have been labeled on the map. The resolved RdRp and PRNTase domains are depicted in slate and cyan, respectively. The four mVP35 protomers with different lengths are shown in different colors: mVP35a is shown in yellow, mVP35b in red, mVP35c in magenta, and mVP35d in orange. b Cartoon representation of MARV L–VP35 complex. MARL and mVP35 are colored as in a. c, d Domain organization of MARL and mVP35. The RdRp domain consists of four subdomains, and they are colored as follows: the N-terminal domain (NTD) is shown in slate, fingers in blue, palm in red, and thumb in green. The densities for the connection domain (CD), methyltransferase (MTase) domain, and C-terminal domain (CTD) are missing in the cryo-EM map and thus are shown in gray. Six conserved regions (CR I–VI) of MARL are labeled based on the sequence alignment of the representative nsNSVs. mVP35 consists of four domains: N-terminal domain (NTD), oligomerization domain (OD), connection region (CR), and C-terminal domain (CTD). mVP35 protomers are colored as in a.

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