5OIX

Structure of the HMPV P oligomerization domain at 1.6 A

5OIX の概要

• エントリーDOI: 10.2210/pdb5oix/pdb
• 分子名称: Phosphoprotein, GLYCEROL (3 entities in total)
• 機能のキーワード: phosphoprotein, p protein, mononegavirales, viral replication, tetramerization, viral protein
• 由来する生物種: Human metapneumovirus
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 106155.60

構造登録者

Renner, M.,Paesen, G.C.,Grison, C.M.,Granier, S.,Grimes, J.M.,Leyrat, C. (登録日: 2017-07-19, 公開日: 2017-11-15, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.61 Å)