期刊
SCIENTIFIC REPORTS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-017-14448-z
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资金
- European Union Seventh Framework Programme (FP7) under SILVER [260644]
- MRC grant [MR/L017709/1]
- Wellcome Trust Fellowship [204703/Z/16/Z]
- Labex EpiGenMed
- Investissements d'avenir' program [ANR-10-LABX-12-01]
- WT [200835/Z/16/Z]
- Wellcome Trust [203141/Z/16/Z]
- Wellcome Trust [204703/Z/16/Z] Funding Source: Wellcome Trust
- MRC [MR/L017709/1] Funding Source: UKRI
- Medical Research Council [MR/L017709/1] Funding Source: researchfish
The phosphoprotein (P) is the main and essential cofactor of the RNA polymerase (L) of nonsegmented, negative-strand RNA viruses. P positions the viral polymerase onto its nucleoproteinRNA 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.
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