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7YOU

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

Summary for 7YOU
Entry DOI10.2210/pdb7you/pdb
EMDB information33987
DescriptorRNA-directed RNA polymerase L, NDV P protein (2 entities in total)
Functional Keywordscryo-em, l-p complex, newcastle disease virus, virus
Biological sourceAvian orthoavulavirus 1
More
Total number of polymer chains5
Total formula weight416136.70
Authors
Chen, Y.,Jingyuan, C.,Xiaoying, F. (deposition date: 2022-08-02, release date: 2023-02-15, Last modification date: 2024-10-23)
Primary citationCong, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.41 Å)
Structure validation

226707

數據於2024-10-30公開中

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