7YOT

Cryo-EM structure of RNA polymerase in complex with P protein tetramer of Newcastle disease virus

Summary for 7YOT

• Entry DOI: 10.2210/pdb7yot/pdb
• EMDB information: 33986
• Descriptor: NDV P protein, RNA-directed RNA polymerase L (2 entities in total)
• Functional Keywords: cryo-em, l-p complex, newcastle disease virus, virus
• Biological source: Avian orthoavulavirus 1; More
• Total number of polymer chains: 5
• Total formula weight: 416136.70

Authors

Chen, Y.,Jingyuan, C. (deposition date: 2022-08-02, release date: 2023-02-15, Last modification date: 2024-10-09)

Primary citation

Cong, J.,Feng, X.,Kang, H.,Fu, W.,Wang, L.,Wang, C.,Li, X.,Chen, Y.,Rao, Z.
Structure of the Newcastle Disease Virus L protein in complex with tetrameric phosphoprotein.
Nat Commun, 14:1324-1324, 2023

PubMed Abstract: Newcastle disease virus (NDV) belongs to Paramyxoviridae, which contains lethal human and animal pathogens. NDV RNA genome is replicated and transcribed by a multifunctional 250 kDa RNA-dependent RNA polymerase (L protein). To date, high-resolution structure of NDV L protein complexed with P protein remains to be elucidated, limiting our understanding of the molecular mechanisms of Paramyxoviridae replication/transcription. Here, we used cryo-EM and enzymatic assays to investigate the structure-function relationship of L-P complex. We found that C-terminal of CD-MTase-CTD module of the atomic-resolution L-P complex conformationally rearranges, and the priming/intrusion loops are likely in RNA elongation conformations different from previous structures. The P protein adopts a unique tetrameric organization and interacts with L protein. Our findings indicate that NDV L-P complex represents elongation state distinct from previous structures. Our work greatly advances the understanding of Paramyxoviridae RNA synthesis, revealing how initiation/elongation alternates, providing clues for identifying therapeutic targets against Paramyxoviridae.

PubMed: 36898997
DOI: 10.1038/s41467-023-37012-y

Experimental method

ELECTRON MICROSCOPY (3 Å)