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Title | Near-Atomic Resolution Structure of a Plant Geminivirus Determined by Electron Cryomicroscopy. |
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Journal, issue, pages | Structure, Vol. 25, Issue 8, Page 1303-11309.e3, Year 2017 |
Publish date | Aug 1, 2017 |
Authors | Katharina Hipp / Clemens Grimm / Holger Jeske / Bettina Böttcher / |
PubMed 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 ...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 links | Structure / PubMed:28712809 |
Methods | EM (single particle) |
Resolution | 4.2 Å |
Structure data | PDB-6ek5: |
Source |
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Keywords | VIRUS / African cassava mosaic virus / Geminivirus / ACMV |