7EJU
Junin virus(JUNV) RNA polymerase L complexed with Z protein
Summary for 7EJU
Entry DOI | 10.2210/pdb7eju/pdb |
EMDB information | 31163 |
Descriptor | RNA-directed RNA polymerase L, RING finger protein Z, ZINC ION, ... (4 entities in total) |
Functional Keywords | junin virus, rna polymerase, l protein, z protein, viral protein |
Biological source | Junin mammarenavirus (Argentinian mammarenavirus, JUNV, Junn mammarenavirus) More |
Total number of polymer chains | 2 |
Total formula weight | 264196.68 |
Authors | Chen, Y. (deposition date: 2021-04-02, release date: 2021-07-07, Last modification date: 2024-10-30) |
Primary citation | Kang, H.,Cong, J.,Wang, C.,Ji, W.,Xin, Y.,Qian, Y.,Li, X.,Chen, Y.,Rao, Z. Structural basis for recognition and regulation of arenavirus polymerase L by Z protein. Nat Commun, 12:4134-4134, 2021 Cited by PubMed Abstract: Junin virus (JUNV) causes Argentine hemorrhagic fever, a debilitating human disease of high mortality rates and a great risk to public health worldwide. Studying the L protein that replicates and transcribes the genome of JUNV, and its regulator Z protein should provide critical clues to identify therapeutic targets for disrupting the life cycle of JUNV. Here we report the 3.54 Å cryo-EM structure of the JUNV L protein complexed with regulator Z protein. JUNV L structure reveals a conserved architecture containing signature motifs found in other L proteins. Structural analysis shows that L protein is regulated by binding of Z protein at the RNA product exit site. Based on these findings, we propose a model for the role of Z protein as a switch to turn on/off the viral RNA synthesis via its interaction with L protein. Our work unveils the mechanism of JUNV transcription, replication and regulation, which provides a framework for the rational design of antivirals for combating viral infections. PubMed: 34226547DOI: 10.1038/s41467-021-24458-1 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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