9r9w

RNA-free helical (h8.5) virus-like particle composed of TEV coat protein

spinqualitylabelsall models 9r9w, resolution 3.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9r9w is a 24 chain structure with sequence from Tobacco etch virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.34Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function POLG_TEV Capsid protein: involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication. Helper component proteinase: required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication. Both 6K peptides are indispensable for virus replication (By similarity). Nuclear inclusion protein A: has RNA-binding and proteolytic activities. Publication Abstract from PubMed Potyviruses are the largest group of plant positive-sense single-stranded RNA viruses and represent a major economic burden worldwide. Their coat protein (CP) forms a filamentous, flexible capsid around the genomic RNA. However, information is still lacking on the mechanisms of virion assembly, disassembly and stability, which is central to understanding virus biology and control. Here, we investigate the role of CP in these processes using structural, biochemical and biophysical studies of five potyviral CPs from three phylogenetic clades combined with bioinformatics and in planta experiments. Our results suggest that, while potyviruses have a conserved virion structure, the amino acids forming the CP-CP and CP-RNA interactions leading to this structure are species-specific. We show that the species-specific CP sequence also determines the architecture of RNA-free virus-like particles (VLPs) and the degree of their structural polymorphism. We identify the residues that determine this specificity at distinct S1-S4 interaction sites. In contrast, a highly conserved charged amino acid triad at the CP-CP interface is essential for the stability of virions and RNA-free VLPs. These results contribute to understanding the molecular mechanism of potyviral virion assembly and highlight the significance of the amino acid sequence of selected CPs in potential biotechnological or biomedical applications. Species-specific structural adaptation of the potyviral coat protein in virions and virus-like particles.,Koritnik N, Kezar A, Kavcic L, Znidaric MT, Leonardi A, De S, Pollari M, Makinen K, Podobnik M Commun Biol. 2026 Jan 13. doi: 10.1038/s42003-025-09502-w. PMID:41530503 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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