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Cell. 2015 Jul 16;162(2):314-327. doi: 10.1016/j.cell.2015.06.018. Epub 2015 Jul 2.

Structure of the L Protein of Vesicular Stomatitis Virus from Electron Cryomicroscopy.

Author information

1
Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 20115, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 20115, USA.
2
Department of Cell Biology, Harvard Medical School, Boston, MA 20115, USA; Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 20115, USA.
3
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 20115, USA.
4
Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 20115, USA.
5
Howard Hughes Medical Institute, Janelia Research Campus, 19700 Helix Drive, Ashburn, VA 20147, USA.
6
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 20115, USA; Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 20115, USA.
7
Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 20115, USA. Electronic address: sean_whelan@hms.harvard.edu.

Abstract

The large (L) proteins of non-segmented, negative-strand RNA viruses, a group that includes Ebola and rabies viruses, catalyze RNA-dependent RNA polymerization with viral ribonucleoprotein as template, a non-canonical sequence of capping and methylation reactions, and polyadenylation of viral messages. We have determined by electron cryomicroscopy the structure of the vesicular stomatitis virus (VSV) L protein. The density map, at a resolution of 3.8 Å, has led to an atomic model for nearly all of the 2109-residue polypeptide chain, which comprises three enzymatic domains (RNA-dependent RNA polymerase [RdRp], polyribonucleotidyl transferase [PRNTase], and methyltransferase) and two structural domains. The RdRp resembles the corresponding enzymatic regions of dsRNA virus polymerases and influenza virus polymerase. A loop from the PRNTase (capping) domain projects into the catalytic site of the RdRp, where it appears to have the role of a priming loop and to couple product elongation to large-scale conformational changes in L.

PMID:
26144317
PMCID:
PMC4557768
DOI:
10.1016/j.cell.2015.06.018
[Indexed for MEDLINE]
Free PMC Article

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