6UCT

Crystal structure of Mal de Rio Cuarto virus P9-1 viroplasm protein (C-arm deletion mutant)

6UCT の概要

• エントリーDOI: 10.2210/pdb6uct/pdb
• 分子名称: p9-1 (1 entity in total)
• 機能のキーワード: fijivirus, mrcv, wheat, maize, reoviridae, viroplasm, viral protein
• 由来する生物種: Mal de Rio Cuarto virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37256.88

構造登録者

Llauger, G.,Klinke, S.,Monti, D.,Sycz, G.,Cerutti, M.L.,Goldbaum, F.A.,del Vas, M.,Otero, L.H. (登録日: 2019-09-17, 公開日: 2021-03-17, 最終更新日: 2026-02-18)

主引用文献

Llauger, G.,Melero, R.,Monti, D.,Sycz, G.,Huck-Iriart, C.,Cerutti, M.L.,Klinke, S.,Mikkelsen, E.,Tijman, A.,Arranz, R.,Alfonso, V.,Arellano, S.M.,Goldbaum, F.A.,Sterckx, Y.G.J.,Carazo, J.M.,Kaufman, S.B.,Dans, P.D.,Del Vas, M.,Otero, L.H.
A Fijivirus Major Viroplasm Protein Shows RNA-Stimulated ATPase Activity by Adopting Pentameric and Hexameric Assemblies of Dimers.
Mbio, 14:e0002323-e0002323, 2023

PubMed Abstract: Fijiviruses replicate and package their genomes within viroplasms in a process involving RNA-RNA and RNA-protein interactions. Here, we demonstrate that the 24 C-terminal residues (C-arm) of the P9-1 major viroplasm protein of the mal de Río Cuarto virus (MRCV) are required for its multimerization and the formation of viroplasm-like structures. Using an integrative structural approach, the C-arm was found to be dispensable for P9-1 dimer assembly but essential for the formation of pentamers and hexamers of dimers (decamers and dodecamers), which favored RNA binding. Although both P9-1 and P9-1ΔC-arm catalyzed ATP with similar activities, an RNA-stimulated ATPase activity was only detected in the full-length protein, indicating a C-arm-mediated interaction between the ATP catalytic site and the allosteric RNA binding sites in the (do)decameric assemblies. A stronger preference to bind phosphate moieties in the decamer was predicted, suggesting that the allosteric modulation of ATPase activity by RNA is favored in this structural conformation. Our work reveals the structural versatility of a fijivirus major viroplasm protein and provides clues to its mechanism of action. The mal de Río Cuarto virus (MRCV) causes an important maize disease in Argentina. MRCV replicates in several species of plants and planthopper vectors. The viral factories, also called viroplasms, have been studied in detail in animal reovirids. This work reveals that a major viroplasm protein of MRCV forms previously unidentified structural arrangements and provides evidence that it may simultaneously adopt two distinct quaternary assemblies. Furthermore, our work uncovers an allosteric communication between the ATP and RNA binding sites that is favored in the multimeric arrangements. Our results contribute to the understanding of plant reovirids viroplasm structure and function and pave the way for the design of antiviral strategies for disease control.

PubMed: 36786587
DOI: 10.1128/mbio.00023-23

実験手法

X-RAY DIFFRACTION (3.47 Å)