Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	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.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 6910, Year 2024
Publish date	Aug 19, 2024
Authors	Benoît Arragain / Tim Krischuns / Martin Pelosse / Petra Drncova / Martin Blackledge / Nadia Naffakh / Stephen Cusack /
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 ...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.
External links	Nat Commun / PubMed:39160148 / PubMed Central
Methods	EM (single particle)
Resolution	2.54 - 3.64 Å
Structure data	19366 8rmp EMDB-19366, PDB-8rmp: Influenza polymerase A/H7N9-4M (ENDO(R) \| Core1) Method: EM (single particle) / Resolution: 2.77 Å 19367 8rmq EMDB-19367, PDB-8rmq: Influenza polymerase A/H7N9-4M (ENDO(R) \| Core2) Method: EM (single particle) / Resolution: 2.54 Å 19368 8rmr EMDB-19368, PDB-8rmr: Influenza polymerase A/H7N9-4M replication complex, an asymmetric polymerase dimer bound to human ANP32A Method: EM (single particle) / Resolution: 3.25 Å 19369 8rms EMDB-19369, PDB-8rms: Influenza polymerase A/H7N9-4M replicase minus 627(R) (from "Influenza polymerase A/H7N9-4M replication complex" \| Local refinement) Method: EM (single particle) / Resolution: 3.21 Å 19382 8rn0 EMDB-19382, PDB-8rn0: Influenza polymerase A/H7N9-4M encapsidase plus 627(R) / human ANP32A (from "Influenza polymerase A/H7N9-4M replication complex" \| Local refinement) Method: EM (single particle) / Resolution: 3.13 Å 19383 8rn1 EMDB-19383, PDB-8rn1: Influenza B polymerase, monomeric encapsidase with 5' cRNA hook bound Method: EM (single particle) / Resolution: 3.64 Å 19384 8rn2 EMDB-19384, PDB-8rn2: Monomeric apo-influenza B polymerase, encapsidase conformation Method: EM (single particle) / Resolution: 2.89 Å 19385 8rn3 EMDB-19385, PDB-8rn3: Pseudo-symmetrical influenza B polymerase apo-dimer, encapsidase moiety (from "Influenza B polymerase pseudo-symmetrical dimer" \| Local refinement) Method: EM (single particle) / Resolution: 2.78 Å 19386 8rn4 EMDB-19386, PDB-8rn4: Pseudo-symmetrical influenza B polymerase apo-dimer, ENDO(T) moiety (from "Influenza B polymerase pseudo-symmetrical dimer" \| Local refinement) Method: EM (single particle) / Resolution: 2.87 Å 19387 8rn5 EMDB-19387, PDB-8rn5: Pseudo-symmetrical influenza B polymerase apo-dimer, ENDO(R) moiety (from "Influenza B polymerase pseudo-symmetrical dimer" \| Local refinement) Method: EM (single particle) / Resolution: 2.88 Å 19388 8rn6 EMDB-19388, PDB-8rn6: Pseudo-symmetrical influenza B polymerase apo-dimer, ENDO(E) moiety (from "Influenza B polymerase pseudo-symmetrical dimer" \| Local refinement) Method: EM (single particle) / Resolution: 2.82 Å 19389 8rn7 EMDB-19389, PDB-8rn7: Pseudo-symmetrical influenza B polymerase apo-dimer, core-only moeity (from "Influenza B polymerase pseudo-symmetrical dimer" \| Local refinement) Method: EM (single particle) / Resolution: 3.09 Å 19390 8rn8 EMDB-19390, PDB-8rn8: Influenza B polymerase pseudo-symmetrical apo-dimer (FluPol(E)\|FluPol(S)) Method: EM (single particle) / Resolution: 2.92 Å 19391 8rn9 EMDB-19391, PDB-8rn9: Influenza B polymerase, replicase (from "Influenza B polymerase apo-trimer" \| Local refinement) Method: EM (single particle) / Resolution: 3.31 Å 19392 8rna EMDB-19392, PDB-8rna: Influenza B polymerase apo-trimer Method: EM (single particle) / Resolution: 3.57 Å 19393 8rnb EMDB-19393, PDB-8rnb: Influenza B polymerase, encapsidase plus 627(R) / human ANP32A (from "Influenza B polymerase apo-trimer" \| Local refinement) Method: EM (single particle) / Resolution: 3.31 Å 19394 8rnc EMDB-19394, PDB-8rnc: Influenza B polymerase, replication complex, an asymmetric polymerase dimer bound to human ANP32A (from "Influenza B polymerase apo-trimer" \| Local refinement) Method: EM (single particle) / Resolution: 3.52 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-HOH: WATER
Source	influenza a virus (a/zhejiang/dtid-zju01/2013(h7n9)) homo sapiens (human) influenza b virus (b/memphis/13/2003)
Keywords	VIRAL PROTEIN / Viral polymerase