5A22
Structure of the L protein of vesicular stomatitis virus from electron cryomicroscopy
Summary for 5A22
| Entry DOI | 10.2210/pdb5a22/pdb |
| EMDB information | 6337 |
| Descriptor | VESICULAR STOMATITIS VIRUS L POLYMERASE, ZINC ION (2 entities in total) |
| Functional Keywords | transferase, rna-dependent rna polymerase, rna capping, cryoem single- particle analysis |
| Biological source | VESICULAR STOMATITIS VIRUS |
| Total number of polymer chains | 1 |
| Total formula weight | 241444.68 |
| Authors | Liang, B.,Li, Z.,Jenni, S.,Rameh, A.A.,Morin, B.M.,Grant, T.,Grigorieff, N.,Harrison, S.C.,Whelan, S.P.J. (deposition date: 2015-05-06, release date: 2015-08-19, Last modification date: 2024-10-23) |
| Primary citation | Liang, B.,Li, Z.,Jenni, S.,Rahmeh, A.A.,Morin, B.M.,Grant, T.,Grigorieff, N.,Harrison, S.C.,Whelan, S.P. Structure of the L Protein of Vesicular Stomatitis Virus from Electron Cryomicroscopy. Cell(Cambridge,Mass.), 162:314-, 2015 Cited by 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 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. PubMed: 26144317DOI: 10.1016/J.CELL.2015.06.018 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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