Structural highlights
Function
[CAPSD_CLVK] Encapsidates the viral DNA into characteristic twinned ('geminate') particles. Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus. The CP of bipartite geminiviruses is not required for cell-to-cell or systemic movement.
Publication Abstract from PubMed
African cassava mosaic virus is a whitefly-transmitted geminivirus which forms unique twin particles of incomplete icosahedra that are joined at five-fold vertices, building an unusual waist. How its 22 capsomers interact within a half-capsid or across the waist is unknown thus far. Using electron cryo-microscopy and image processing, we determined the virion structure with a resolution of 4.2 A and built an atomic model for its capsid protein. The inter-capsomer contacts mediated by the flexible N termini and loop regions differed within the half-capsids and at the waist, explaining partly the unusual twin structure. The tip of the pentameric capsomer is sealed by a plug formed by a turn region harboring the evolutionary conserved residue Y193. Basic amino acid residues inside the capsid form a positively charged pocket next to the five-fold axis of the capsomer suitable for binding DNA. Within this pocket, density most likely corresponding to DNA was resolved.
Near-Atomic Resolution Structure of a Plant Geminivirus Determined by Electron Cryomicroscopy.,Hipp K, Grimm C, Jeske H, Bottcher B Structure. 2017 Aug 1;25(8):1303-1309.e3. doi: 10.1016/j.str.2017.06.013. Epub, 2017 Jul 14. PMID:28712809[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hipp K, Grimm C, Jeske H, Bottcher B. Near-Atomic Resolution Structure of a Plant Geminivirus Determined by Electron Cryomicroscopy. Structure. 2017 Aug 1;25(8):1303-1309.e3. doi: 10.1016/j.str.2017.06.013. Epub, 2017 Jul 14. PMID:28712809 doi:https://dx.doi.org/10.1016/j.str.2017.06.013
