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8RN0

Influenza polymerase A/H7N9-4M encapsidase plus 627(R) / human ANP32A (from "Influenza polymerase A/H7N9-4M replication complex" | Local refinement)

Summary for 8RN0
Entry DOI10.2210/pdb8rn0/pdb
EMDB information19382
DescriptorPolymerase basic protein 2, Polymerase acidic protein, RNA-directed RNA polymerase catalytic subunit, ... (4 entities in total)
Functional Keywordsviral polymerase, viral protein
Biological sourceInfluenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))
More
Total number of polymer chains5
Total formula weight379076.55
Authors
Arragain, B.,Cusack, S. (deposition date: 2024-01-09, release date: 2024-09-11)
Primary citationArragain, B.,Krischuns, T.,Pelosse, M.,Drncova, P.,Blackledge, M.,Naffakh, N.,Cusack, S.
Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase.
Nat Commun, 15:6910-6910, 2024
Cited by
PubMed Abstract: Replication of influenza viral RNA depends on at least two viral polymerases, a parental replicase and an encapsidase, and cellular factor ANP32. ANP32 comprises an LRR domain and a long C-terminal low complexity acidic region (LCAR). Here we present evidence suggesting that ANP32 is recruited to the replication complex as an electrostatic chaperone that stabilises the encapsidase moiety within apo-polymerase symmetric dimers that are distinct for influenza A and B polymerases. The ANP32 bound encapsidase, then forms the asymmetric replication complex with the replicase, which is embedded in a parental ribonucleoprotein particle (RNP). Cryo-EM structures reveal the architecture of the influenza A and B replication complexes and the likely trajectory of the nascent RNA product into the encapsidase. The cryo-EM map of the FluB replication complex shows extra density attributable to the ANP32 LCAR wrapping around and stabilising the apo-encapsidase conformation. These structures give new insight into the various mutations that adapt avian strain polymerases to use the distinct ANP32 in mammalian cells.
PubMed: 39160148
DOI: 10.1038/s41467-024-51007-3
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.13 Å)
Structure validation

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PDB entries from 2024-11-13

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