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| Title | Structure of the L Protein of Vesicular Stomatitis Virus from Electron Cryomicroscopy. |
|---|---|
| Journal, issue, pages | Cell, Vol. 162, Issue 2, Page 314-327, Year 2015 |
| Publish date | Jul 16, 2015 |
 Authors | Bo Liang / Zongli Li / Simon Jenni / Amal A Rahmeh / Benjamin M Morin / Timothy Grant / Nikolaus Grigorieff / Stephen C Harrison / Sean P J Whelan /  |
| PubMed 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 ...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. |
 External links | Cell / PubMed:26144317 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.8 Å |
| Structure data | |
| Chemicals |  ChemComp-ZN: |
| Source |
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 Keywords |  TRANSFERASE / RNA-DEPENDENT RNA POLYMERASE / RNA CAPPING / CRYOEM SINGLE- PARTICLE ANALYSIS |
