Extended Data Fig. 9: The η7 helix in the viral polymerase cavity is conserved among different viruses. | Nature Structural & Molecular Biology

Extended Data Fig. 9: The η7 helix in the viral polymerase cavity is conserved among different viruses.

From: An intermediate state allows influenza polymerase to switch smoothly between transcription and replication cycles

Extended Data Fig. 9

The RdRp regions in RABV (rabies virus, PDB: 6UEB), VSV (vesicular stomatitis virus, PDB: 6U1X), HRSV (human respiratory syncytial virus, PDB: 6PZK), HMPV (human metapneumovirus, PDB: 6U5O), HPIV (human parainfluenza virus, PDB: 6V85), LACV (La Crosse orthobunyavirus, PDB: 5AMQ), LASV (Lassa mammarenavirus, PDB: 6KLC), MACV (Machupo mammarenavirus, PDB: 6KLD) and SFTSV (thrombocytopaenia syndrome virus, PDB: 6Y6K) polymerases are shown as same orientation in cartoon representation (green). The positions of fingers, palm and thumb subdomains are labeled. The homologous structures of η7 helix (in blue) are found in all of these polymerases. Despite of sequence variability, bulky residues like phenylalanine, tryptophan and arginine, are observed at the homologous position of Met507 and Glu508 in influenza polymerase.

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