6UEB

Structure of Rabies SAD-B19 L-P complex from cryo-EM

Summary for 6UEB

• Entry DOI: 10.2210/pdb6ueb/pdb
• EMDB information: 20753
• Descriptor: Large structural protein, Phosphoprotein,Phosphoprotein, ZINC ION (3 entities in total)
• Functional Keywords: polymerase, phosphoprotein, complex, viral protein
• Biological source: Rabies virus (strain SAD B19) (RABV); More
• Total number of polymer chains: 2
• Total formula weight: 248028.20

Authors

Horwitz, J.A.,Harrison, S.C. (deposition date: 2019-09-20, release date: 2020-02-05, Last modification date: 2024-03-20)

Primary citation

Horwitz, J.A.,Jenni, S.,Harrison, S.C.,Whelan, S.P.J.
Structure of a rabies virus polymerase complex from electron cryo-microscopy.
Proc.Natl.Acad.Sci.USA, 117:2099-2107, 2020

PubMed Abstract: Nonsegmented negative-stranded (NNS) RNA viruses, among them the virus that causes rabies (RABV), include many deadly human pathogens. The large polymerase (L) proteins of NNS RNA viruses carry all of the enzymatic functions required for viral messenger RNA (mRNA) transcription and replication: RNA polymerization, mRNA capping, and cap methylation. We describe here a complete structure of RABV L bound with its phosphoprotein cofactor (P), determined by electron cryo-microscopy at 3.3 Å resolution. The complex closely resembles the vesicular stomatitis virus (VSV) L-P, the one other known full-length NNS-RNA L-protein structure, with key local differences (e.g., in L-P interactions). Like the VSV L-P structure, the RABV complex analyzed here represents a preinitiation conformation. Comparison with the likely elongation state, seen in two structures of pneumovirus L-P complexes, suggests differences between priming/initiation and elongation complexes. Analysis of internal cavities within RABV L suggests distinct template and product entry and exit pathways during transcription and replication.

PubMed: 31953264
DOI: 10.1073/pnas.1918809117

Experimental method

ELECTRON MICROSCOPY (3.3 Å)