7kvc

Cryo-EM structure of Mal de Rio Cuarto virus P9-1 viroplasm protein (decamer)Cryo-EM structure of Mal de Rio Cuarto virus P9-1 viroplasm protein (decamer)

Structural highlights 7kvc is a 10 chain structure with sequence from Mal de Rio Cuarto virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.7Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D9U542_9REOV Publication Abstract from PubMed 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 Rio 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 P9-1DeltaC-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. IMPORTANCE The mal de Rio Cuarto virus (MRCV) causes an important maize disease in Argentina. MRCV replicates in several species of Gramineae 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. A Fijivirus Major Viroplasm Protein Shows RNA-Stimulated ATPase Activity by Adopting Pentameric and Hexameric Assemblies of Dimers.,Llauger G, Melero R, Monti D, Sycz G, Huck-Iriart C, Cerutti ML, Klinke S, Mikkelsen E, Tijman A, Arranz R, Alfonso V, Arellano SM, Goldbaum FA, Sterckx YGJ, Carazo JM, Kaufman SB, Dans PD, Del Vas M, Otero LH mBio. 2023 Apr 25;14(2):e0002323. doi: 10.1128/mbio.00023-23. Epub 2023 Feb 14. PMID:36786587 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 7kvc, resolution 4.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image