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

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: 26144317
DOI: 10.1016/J.CELL.2015.06.018

Experimental method

ELECTRON MICROSCOPY (3.8 Å)