6EK5

Near-atomic resolution structure of a plant geminivirus determined by electron cryo-microscopy.

This is a non-PDB format compatible entry.

Replaces:  5MJF

Summary for 6EK5

• Entry DOI: 10.2210/pdb6ek5/pdb
• EMDB information: 3521
• Descriptor: Capsid protein (1 entity in total)
• Functional Keywords: african cassava mosaic virus, geminivirus, acmv, virus
• Biological source: African cassava mosaic virus (ACMV)
• Total number of polymer chains: 110
• Total formula weight: 2650438.01

Authors

Grimm, C.,Bottcher, B.,Hipp, K.,Jeske, H. (deposition date: 2017-09-25, release date: 2017-10-11, Last modification date: 2024-07-10)

Primary citation

Hipp, K.,Grimm, C.,Jeske, H.,Bottcher, B.
Near-Atomic Resolution Structure of a Plant Geminivirus Determined by Electron Cryomicroscopy.
Structure, 25:1303-1309.e3, 2017

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 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.

PubMed: 28712809
DOI: 10.1016/j.str.2017.06.013

Experimental method

ELECTRON MICROSCOPY (4.2 Å)