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PDBsum entry 6klc
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Viral protein
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PDB id
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6klc
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References listed in PDB file
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Key reference
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Title
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Structural insight into arenavirus replication machinery.
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Authors
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R.Peng,
X.Xu,
J.Jing,
M.Wang,
Q.Peng,
S.Liu,
Y.Wu,
X.Bao,
P.Wang,
J.Qi,
G.F.Gao,
Y.Shi.
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Ref.
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Nature, 2020,
579,
615-619.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Arenaviruses can cause severe haemorrhagic fever and neurological diseases in
humans and other animals, exemplified by Lassa mammarenavirus, Machupo
mammarenavirus and lymphocytic choriomeningitis virus, posing great threats to
public health1-4. These viruses encode a large multi-domain
RNA-dependent RNA polymerase for transcription and replication of the viral
genome5. Viral polymerases are one of the leading antiviral
therapeutic targets. However, the structure of arenavirus polymerase is not yet
known. Here we report the near-atomic resolution structures of Lassa and Machupo
virus polymerases in both apo and promoter-bound forms. These structures display
a similar overall architecture to influenza virus and bunyavirus polymerases but
possess unique local features, including an arenavirus-specific insertion domain
that regulates the polymerase activity. Notably, the ordered active site of
arenavirus polymerase is inherently switched on, without the requirement for
allosteric activation by 5'-viral RNA, which is a necessity for both influenza
virus and bunyavirus polymerases6,7. Moreover, dimerization could
facilitate the polymerase activity. These findings advance our understanding of
the mechanism of arenavirus replication and provide an important basis for
developing antiviral therapeutics.
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