7VH1

Cryo-EM structure of Machupo virus dimeric L-Z complex

Summary for 7VH1

• Entry DOI: 10.2210/pdb7vh1/pdb
• EMDB information: 31975 31983
• Descriptor: RNA-directed RNA polymerase L, Maltose/maltodextrin-binding periplasmic protein,RING finger protein Z, ZINC ION (3 entities in total)
• Functional Keywords: polymerase, matrix protein, complex, viral protein
• Biological source: Machupo virus (MACV); More
• Total number of polymer chains: 2
• Total formula weight: 308501.05

Authors

Zhang, X.,Ma, J.,Zhang, S. (deposition date: 2021-09-20, release date: 2021-09-29, Last modification date: 2024-10-16)

Primary citation

Ma, J.,Zhang, S.,Zhang, X.
Structure of Machupo virus polymerase in complex with matrix protein Z.
Nat Commun, 12:6163-6163, 2021

PubMed Abstract: The Arenaviridae family includes several viruses that cause severe human hemorrhagic fevers with high mortality, with no effective countermeasures currently available. The arenavirus multi-domain L protein is involved in viral transcription and replication and represents a promising target for antiviral drugs. The arenavirus matrix protein Z is a small multi-functional protein that inhibits the activities of the L protein. Here we report the structure of Machupo virus L protein in complex with Z determined by cryo-electron microscopy. The Z protein acts as a staple and binds the L protein with 1:1 stoichiometry at the intersection between the PA-C-like region, RNA-dependent RNA polymerase and PB2-N-like region. Binding of the Z protein may lock the multiple domains of L into a fixed arrangement leading to loss of catalytic activity. These results further our understanding of the inhibitory mechanism of arenavirus replication machinery and provide a novel perspective to develop antiviral drugs.

PubMed: 34697302
DOI: 10.1038/s41467-021-26432-3

Experimental method

ELECTRON MICROSCOPY (4.2 Å)