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	Structure of the N-RNA/P interface indicates mode of L/P recruitment to the nucleocapsid of human metapneumovirus.
Journal, issue, pages	Nat Commun, Vol. 14, Issue 1, Page 7627, Year 2023
Publish date	Nov 22, 2023
Authors	Jack D Whitehead / Hortense Decool / Cédric Leyrat / Loic Carrique / Jenna Fix / Jean-François Eléouët / Marie Galloux / Max Renner /
PubMed Abstract	Human metapneumovirus (HMPV) is a major cause of respiratory illness in young children. The HMPV polymerase (L) binds an obligate cofactor, the phosphoprotein (P). During replication and ...Human metapneumovirus (HMPV) is a major cause of respiratory illness in young children. The HMPV polymerase (L) binds an obligate cofactor, the phosphoprotein (P). During replication and transcription, the L/P complex traverses the viral RNA genome, which is encapsidated within nucleoproteins (N). An essential interaction between N and a C-terminal region of P tethers the L/P polymerase to the template. This N-P interaction is also involved in the formation of cytoplasmic viral factories in infected cells, called inclusion bodies. To define how the polymerase component P recognizes N-encapsidated RNA (N-RNA) we employed cryogenic electron microscopy (cryo-EM) and molecular dynamics simulations, coupled to activity assays and imaging of inclusion bodies in cells. We report a 2.9 Å resolution structure of a triple-complex between multimeric N, bound to both RNA and the C-terminal region of P. Furthermore, we also present cryo-EM structures of assembled N in different oligomeric states, highlighting the plasticity of N. Combined with our functional assays, these structural data delineate in molecular detail how P attaches to N-RNA whilst retaining substantial conformational dynamics. Moreover, the N-RNA-P triple complex structure provides a molecular blueprint for the design of therapeutics to potentially disrupt the attachment of L/P to its template.
External links	Nat Commun / PubMed:37993464 / PubMed Central
Methods	EM (single particle)
Resolution	2.9 - 4.7 Å
Structure data	17613 8pdl EMDB-17613, PDB-8pdl: 10-mer ring of human metapneumovirus (HMPV) N-RNA Method: EM (single particle) / Resolution: 3.1 Å 17614 8pdm EMDB-17614, PDB-8pdm: 11-mer ring of human metapneumovirus (HMPV) N-RNA Method: EM (single particle) / Resolution: 3.3 Å 17615 8pdn EMDB-17615, PDB-8pdn: Spiral of assembled human metapneumovirus (HMPV) N-RNA Method: EM (single particle) / Resolution: 4.7 Å 17616 8pdo EMDB-17616, PDB-8pdo: Local refinement of dimeric human metapneumovirus (HMPV) N-RNA Method: EM (single particle) / Resolution: 3.1 Å 17617 8pdp EMDB-17617, PDB-8pdp: 10-mer ring of HMPV N-RNA bound to the C-terminal region of P Method: EM (single particle) / Resolution: 2.9 Å 17618 8pdq EMDB-17618, PDB-8pdq: 11-mer ring of HMPV N-RNA bound to the C-terminal region of P Method: EM (single particle) / Resolution: 3.1 Å 17619 8pdr EMDB-17619, PDB-8pdr: Rigid body fit of assembled HMPV N-RNA spiral bound to the C-terminal region of P Method: EM (single particle) / Resolution: 4.0 Å 17620 8pds EMDB-17620, PDB-8pds: Local refinement of dimeric HMPV N-RNA bound to the C-terminal region of P Method: EM (single particle) / Resolution: 2.9 Å
Source	human metapneumovirus (strain can97-83) escherichia coli (E. coli) uman metapneumovirus (strain can97-83)
Keywords	VIRAL PROTEIN / Nucleoprotein / Virus / Nucleocapsid / RNA-binding / HMPV / Pneumoviridae / Mononegavirales