6ek5

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.