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TitleNear-Atomic Resolution Structure of a Plant Geminivirus Determined by Electron Cryomicroscopy.
Journal, issue, pagesStructure, Vol. 25, Issue 8, Page 1303-11309.e3, Year 2017
Publish dateAug 1, 2017
AuthorsKatharina Hipp / Clemens Grimm / Holger Jeske / Bettina Böttcher /
PubMed AbstractAfrican 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 ...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.
External linksStructure / PubMed:28712809
MethodsEM (single particle)
Resolution4.2 Å
Structure data

PDB-6ek5:
Near-atomic resolution structure of a plant geminivirus determined by electron cryo-microscopy.
Method: ELECTRON MICROSCOPY / Resolution: 4.2 Å

Source
  • african cassava mosaic virus
KeywordsVIRUS / African cassava mosaic virus / Geminivirus / ACMV

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