EMD-6337

Single-particle
3.8 Å
EMD-6337 Deposition: 07/05/2015
Map released: 20/05/2015
Last modified: 19/08/2015
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-6337

Structure of the L-protein of vesicular stomatitis virus from electron cryomicroscopy

EMD-6337

Single-particle
3.8 Å
EMD-6337 Deposition: 07/05/2015
Map released: 20/05/2015
Last modified: 19/08/2015
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Vesicular stomatitis virus
Sample: VSV-L
Fitted models: 5a22 (Avg. Q-score: 0.396)

Deposition Authors: Liang B , Li Z, Jenni S, Rameh AA , Morin BM, Grant T , Grigorieff N , Harrison SC, Whelan SPJ
Structure of the L-protein of vesicular stomatitis virus from electron cryomicroscopy
Liang B , Li Z, Jenni S, Rameh AA , Morin BM, Grant T , Grigorieff N , Harrison SC, Whelan SPJ
(2015) Cell , 162 , 314 - 327
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.