Structural highlights
Function
Q91KZ5_9MONO
Publication Abstract from PubMed
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.
Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering.,Renner M, Paesen GC, Grison CM, Granier S, Grimes JM, Leyrat C Sci Rep. 2017 Nov 1;7(1):14865. doi: 10.1038/s41598-017-14448-z. PMID:29093501[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Renner M, Paesen GC, Grison CM, Granier S, Grimes JM, Leyrat C. Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering. Sci Rep. 2017 Nov 1;7(1):14865. doi: 10.1038/s41598-017-14448-z. PMID:29093501 doi:http://dx.doi.org/10.1038/s41598-017-14448-z
