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-Structure paper
Title | Structure of Machupo virus polymerase in complex with matrix protein Z. |
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Journal, issue, pages | Nat Commun, Vol. 12, Issue 1, Page 6163, Year 2021 |
Publish date | Oct 25, 2021 |
Authors | Jun Ma / Shuangyue Zhang / Xinzheng Zhang / |
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 ...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. |
External links | Nat Commun / PubMed:34697302 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.6 - 5.1 Å |
Structure data | EMDB-31975, PDB-7vgq: EMDB-31983, PDB-7vh1: EMDB-31984, PDB-7vh2: EMDB-31985, PDB-7vh3: |
Chemicals | ChemComp-ZN: |
Source |
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Keywords | VIRAL PROTEIN / Polymerase / matrix protein / complex |