EMD-6337
Structure of the L-protein of vesicular stomatitis virus from electron cryomicroscopy
EMD-6337
Single-particle3.8 Å
![EMD-6337](https://www.ebi.ac.uk/emdb/images/entry/EMD-6337/400_6337.gif)
Map released: 20/05/2015
Last modified: 19/08/2015
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
Sample: VSV-L
Fitted models: 5a22 (Avg. Q-score: 0.396)
Deposition Authors: Liang B
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![](http://www.ebi.ac.uk/web_guidelines/images/logos/orcid/orcid_16x16.png)
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
![](http://www.ebi.ac.uk/web_guidelines/images/logos/orcid/orcid_16x16.png)
![](http://www.ebi.ac.uk/web_guidelines/images/logos/orcid/orcid_16x16.png)
![](http://www.ebi.ac.uk/web_guidelines/images/logos/orcid/orcid_16x16.png)
![](http://www.ebi.ac.uk/web_guidelines/images/logos/orcid/orcid_16x16.png)
![](http://www.ebi.ac.uk/web_guidelines/images/logos/orcid/orcid_16x16.png)
(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.
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.