5OIX

Structure of the HMPV P oligomerization domain at 1.6 A

Summary for 5OIX

• Entry DOI: 10.2210/pdb5oix/pdb
• Descriptor: Phosphoprotein, GLYCEROL (3 entities in total)
• Functional Keywords: phosphoprotein, p protein, mononegavirales, viral replication, tetramerization, viral protein
• Biological source: Human metapneumovirus
• Total number of polymer chains: 8
• Total formula weight: 106155.60

Authors

Renner, M.,Paesen, G.C.,Grison, C.M.,Granier, S.,Grimes, J.M.,Leyrat, C. (deposition date: 2017-07-19, release date: 2017-11-15, Last modification date: 2024-05-08)

Primary citation

Renner, M.,Paesen, G.C.,Grison, C.M.,Granier, S.,Grimes, J.M.,Leyrat, C.
Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering.
Sci Rep, 7:14865-14865, 2017

PubMed 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 (P) flanked by large intrinsically disordered regions (IDRs). Here we combined x-ray crystallography of P 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.

PubMed: 29093501
DOI: 10.1038/s41598-017-14448-z

Experimental method

X-RAY DIFFRACTION (1.61 Å)