Near-Atomic Resolution Structure of a Plant Geminivirus Determined by Electron 
Cryomicroscopy

Hipp, K; Grimm, C; Jeske, H; Böttcher, B

doi:10.1016/j.str.2017.06.013

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Near-Atomic Resolution Structure of a Plant Geminivirus Determined by Electron Cryomicroscopy

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Hipp, K., Grimm, C., Jeske, H., & Böttcher, B. (2017). Near-Atomic Resolution Structure of a Plant Geminivirus Determined by Electron Cryomicroscopy. Structure, 25(8), 1303-1309. doi:10.1016/j.str.2017.06.013.

Cite as: https://hdl.handle.net/21.11116/0000-000C-4510-4

Abstract

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 Å 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.