Journal
STRUCTURE
Volume 25, Issue 8, Pages 1303-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2017.06.013
Keywords
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Funding
- Senator-Eiselen-Vermachtnis
- DFG [Je 116/11-1]
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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 cryomicroscopy and image processing, we determined the virion structure with a resolution of 4.2 angstrom 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.
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