Negative-strand (NS) RNA viruses initiate infection with a unique polymerase complex. This protein complex mediates both mRNA transcription and subsequent genomic RNA replication. Domains for both functional interactions are contained within a single Large polymerase protein (L-protein).
Protein Description 5A22
Large Protein (L-protein) RNA viruses include both Ebola and rabies viruses. 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.
Biologic Explorer 5A22
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.
Biologic model of L-protein of Vesicular Stomatitis Virus 5A22 3D printed in Multi-colored Plastic and Full-color Sandstone.