6UEN

Cryo-EM structure of the respiratory syncytial virus RNA polymerase

Summary for 6UEN

• Entry DOI: 10.2210/pdb6uen/pdb
• EMDB information: 20754
• Descriptor: RNA-directed RNA polymerase L, the phosphoprotein (P) of human respiratory syncytial virus (2 entities in total)
• Functional Keywords: viral protein complexes, viral protein, viral protein-transferase complex, viral protein/transferase
• Biological source: Human respiratory syncytial virus; More
• Total number of polymer chains: 5
• Total formula weight: 282249.95

Authors

Cao, D.,Gao, Y.,Liang, B. (deposition date: 2019-09-22, release date: 2020-01-22, Last modification date: 2024-03-20)

Primary citation

Cao, D.,Gao, Y.,Roesler, C.,Rice, S.,D'Cunha, P.,Zhuang, L.,Slack, J.,Domke, M.,Antonova, A.,Romanelli, S.,Keating, S.,Forero, G.,Juneja, P.,Liang, B.
Cryo-EM structure of the respiratory syncytial virus RNA polymerase.
Nat Commun, 11:368-368, 2020

PubMed Abstract: The respiratory syncytial virus (RSV) RNA polymerase, constituted of a 250 kDa large (L) protein and tetrameric phosphoprotein (P), catalyzes three distinct enzymatic activities - nucleotide polymerization, cap addition, and cap methylation. How RSV L and P coordinate these activities is poorly understood. Here, we present a 3.67 Å cryo-EM structure of the RSV polymerase (L:P) complex. The structure reveals that the RNA dependent RNA polymerase (RdRp) and capping (Cap) domains of L interact with the oligomerization domain (P) and C-terminal domain (P) of a tetramer of P. The density of the methyltransferase (MT) domain of L and the N-terminal domain of P (P) is missing. Further analysis and comparison with other RNA polymerases at different stages suggest the structure we obtained is likely to be at an elongation-compatible stage. Together, these data provide enriched insights into the interrelationship, the inhibitors, and the evolutionary implications of the RSV polymerase.

PubMed: 31953395
DOI: 10.1038/s41467-019-14246-3

Experimental method

ELECTRON MICROSCOPY (3.67 Å)