5CHS

N-terminal domain of the vesicular stomatitis virus L protein

Summary for 5CHS

• Entry DOI: 10.2210/pdb5chs/pdb
• Descriptor: RNA-directed RNA polymerase L, PENTAETHYLENE GLYCOL, SODIUM ION, ... (4 entities in total)
• Functional Keywords: polymerase, virus, viral protein, transferase
• Biological source: Vesicular stomatitis Indiana virus (VSIV)
• Total number of polymer chains: 2
• Total formula weight: 80914.53

Authors

Green, T.J.,Qiu, S.,Luo, M. (deposition date: 2015-07-10, release date: 2015-07-22, Last modification date: 2024-10-23)

Primary citation

Qiu, S.,Ogino, M.,Luo, M.,Ogino, T.,Green, T.J.
Structure and Function of the N-Terminal Domain of the Vesicular Stomatitis Virus RNA Polymerase.
J.Virol., 90:715-724, 2015

PubMed Abstract: Viruses have various mechanisms to duplicate their genomes and produce virus-specific mRNAs. Negative-strand RNA viruses encode their own polymerases to perform each of these processes. For the nonsegmented negative-strand RNA viruses, the polymerase is comprised of the large polymerase subunit (L) and the phosphoprotein (P). L proteins from members of the Rhabdoviridae, Paramyxoviridae, and Filoviridae share sequence and predicted secondary structure homology. Here, we present the structure of the N-terminal domain (conserved region I) of the L protein from a rhabdovirus, vesicular stomatitis virus, at 1.8-Å resolution. The strictly and strongly conserved residues in this domain cluster in a single area of the protein. Serial mutation of these residues shows that many of the amino acids are essential for viral transcription but not for mRNA capping. Three-dimensional alignments show that this domain shares structural homology with polymerases from other viral families, including segmented negative-strand RNA and double-stranded RNA (dsRNA) viruses.

PubMed: 26512087
DOI: 10.1128/JVI.02317-15

Experimental method

X-RAY DIFFRACTION (1.8 Å)