The 3.3 Å structure of a plant geminivirus using cryo-EM

摘要: Geminiviruses are major plant pathogens that threaten food security globally. They have a unique architecture built from two incomplete icosahedral particles, fused to form geminate capsid. However, despite their importance agricultural economies and fundamental biological interest, the details of how this is realized in 3D remain unknown. Here we report structure Ageratum yellow vein virus at 3.3 A resolution, using single-particle cryo-electron microscopy, together with an atomic model shows N-terminus single capsid protein (CP) adopts three different conformations essential for building interface between halves. Our map also contains density ~7 bases single-stranded DNA bound each CP, show interactions genome CPs than rest With additional mutagenesis data, suggests central role binding-induced conformational change directing assembly capsids.