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Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering

DOI: 10.1038/s41598-017-14448-z DOI Help

Authors: Max Renner (Oxford University) , Guido C. Paesen (Oxford University) , Claire M. Grison (CNRS, University of Montpellier) , Sébastien Granier (CNRS, University of Montpellier) , Jonathan M. Grimes (Oxford University; Diamond Light Source) , Cedric Leyrat (CNRS, University of Montpellier)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Scientific Reports , VOL 7

State: Published (Approved)
Published: November 2017
Diamond Proposal Number(s): 10627

Open Access Open Access

Abstract: The phosphoprotein (P) is the main and essential cofactor of the RNA polymerase (L) of non-segmented, negative‐strand RNA viruses. P positions the viral polymerase onto its nucleoprotein–RNA template and acts as a chaperone of the nucleoprotein (N), thereby preventing nonspecific encapsidation of cellular RNAs. The phosphoprotein of human metapneumovirus (HMPV) forms homotetramers composed of a stable oligomerization domain (Pcore) flanked by large intrinsically disordered regions (IDRs). Here we combined x-ray crystallography of Pcore with small angle x-ray scattering (SAXS)-based ensemble modeling of the full-length P protein and several of its fragments to provide a structural description of P that captures its dynamic character, and highlights the presence of varyingly stable structural elements within the IDRs. We discuss the implications of the structural properties of HMPV P for the assembly and functioning of the viral transcription/replication machinery.

Journal Keywords: Intrinsically disordered proteins; Molecular modelling; SAXS

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Other Facilities: European Synchrotron Radiation Facility

Documents:
s41598-017-14448-z.pdf

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