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

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_core) flanked by large intrinsically disordered regions (IDRs). Here we combined x-ray crystallography of P_core 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 vary

SUBMITTER: Renner M 

PROVIDER: S-EPMC5665942 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature