6f2s

CryoEM structure of Ageratum Yellow Vein virus (AYVV)

spinqualitylabelsall models 6f2s, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6f2s is a 22 chain structure with sequence from [1] and Ayvv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: V1 (AYVV) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [W5RUR4_9GEMI] Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus.[RuleBase:RU363025] Publication Abstract from PubMed Geminiviruses are major plant pathogens that threaten food security globally. They have a unique architecture built from two incomplete icosahedral particles, fused to form a geminate capsid. However, despite their importance to agricultural economies and fundamental biological interest, the details of how this is realized in 3D remain unknown. Here we report the structure of Ageratum yellow vein virus at 3.3 A resolution, using single-particle cryo-electron microscopy, together with an atomic model that shows that the N-terminus of the single capsid protein (CP) adopts three different conformations essential for building the interface between geminate halves. Our map also contains density for ~7 bases of single-stranded DNA bound to each CP, and we show that the interactions between the genome and CPs are different at the interface than in the rest of the capsid. With additional mutagenesis data, this suggests a central role for DNA binding-induced conformational change in directing the assembly of geminate capsids. The 3.3 A structure of a plant geminivirus using cryo-EM.,Hesketh EL, Saunders K, Fisher C, Potze J, Stanley J, Lomonossoff GP, Ranson NA Nat Commun. 2018 Jun 18;9(1):2369. doi: 10.1038/s41467-018-04793-6. PMID:29915210 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA