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We are analyzing https://www.nature.com/articles/s41467-018-04793-6.

Title:
The 3.3 Å structure of a plant geminivirus using cryo-EM | Nature Communications
Description:
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 Å 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. Geminiviruses are an important plant pathogen that causes large food crop losses globally. Here the authors describe a high resolution cryo-EM structure of the Ageratum yellow vein virus and reveal the molecular details of how a single capsid protein sequence can adopt the different conformations needed to build that geminate capsid.
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Keywords {🔍}

dna, article, structure, virus, google, scholar, geminate, capsid, fig, cas, ayvv, interface, resolution, supplementary, nature, density, chain, particles, particle, interactions, model, assembly, geminivirus, subunit, subunits, residues, interaction, single, cryoem, data, plant, binding, genome, cps, nterminal, ordered, conformations, genomic, geminiviruses, yellow, singlestranded, structures, dnaα, motif, conformation, role, disease, dnaa, stnv, chains,

Topics {✒️}

nature portfolio privacy policy vacation research scholarship advertising norwich research park yield peaq-ht-d1-ayvvcp agar scientific single-particle cryo-electron microscopy social media exploratory research electron cryo-microscopy reconstructions tools reprints domain-swapped β-strand interaction low-resolution cryo-em studies improved cryo-electron microscopy helix-loop-helix motif japan africa development nature 422 nature 270 nature 325 nature 276 nature 541 nature” nature helix-turn-helix motif peaq-ht-d1-ayvvcp nupage mops-buffered gels cryo-em data collection single-stranded dna–protein interactions reference-free 2d classification36 classical quasi-equivalence theory9 single-stranded rna virus7 single-stranded rna viruses17 single-stranded rna virus additional mutagenesis data early cryo-em structures virus coat proteins subsequent maldi-tof analysis plant-infecting viruses real-time ctf determination reference-free 2d classification cryo-em structure determination structural molecular biology cryo-em dataset collected n-terminal α-helix antiparallel β-strand interaction single-stranded dna molecule

Questions {❓}

  • Equine rhinitis A virus and its low pH empty particle: clues towards an aphthovirus entry mechanism?
  • Firstly, how does a single CP accommodate the different conformations required to build a geminate particle?
  • However, a fundamental question remains: how does a CP subunit ‘know’ what position it occupies within the overall architecture of the capsid?

Schema {🗺️}

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      headline:The 3.3 Å structure of a plant geminivirus using cryo-EM
      description: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 Å 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. Geminiviruses are an important plant pathogen that causes large food crop losses globally. Here the authors describe a high resolution cryo-EM structure of the Ageratum yellow vein virus and reveal the molecular details of how a single capsid protein sequence can adopt the different conformations needed to build that geminate capsid.
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