Architecture and Evolution of Blade Assembly in β-propeller Lectins

Allbwn ymchwil: Cyfraniad at gyfnodolynErthygl

Fersiynau electronig


  • propeller_full (002)

    Llawysgrif awdur wedi’i dderbyn, 1 MB, dogfen-PDF

    Embargo yn dod i ben: 7/03/20

Dangosydd eitem ddigidol (DOI)

  • Francois Bonnardel
    University of Grenoble Alpes, Grenoble
  • Atal Kumar
    University of Grenoble Alpes, Grenoble
  • Michaela Wimmerova
    Masaryk University, Brno
  • Martina Lahmann
  • Sergei Perez
    University of Grenoble Alpes, Grenoble
  • Annabelle Varrot
    University of Grenoble Alpes, Grenoble
  • Frédérique Lisacek
    Swiss Institute of Bioinformatics, Geneva
  • Anne Imberty
    University of Grenoble Alpes, Grenoble
Lectins with a β-propeller fold bind glycans on the cell surface through multivalent binding sites and appropriate directionality. These proteins are formed by repeats of short domains, raising questions about evolutionary duplication. However, these repeats are difficult to detect in translated genomes and seldom correctly annotated in sequence databases. To address these issues, we defined the blade signature of the five types of β-propellers using 3D-structural data. With these templates, we predicted 3,887 β-propeller lectins in 1,889 species and organized this information in a searchable online database. The data reveal a widespread distribution of β-propeller lectins across species. Prediction also emphasizes multiple architectures and led to the discovery of a β-propeller assembly scenario. This was confirmed by producing and characterizing a predicted protein coded in the genome of Kordia zhangzhouensis. The crystal structure uncovers an intermediate in the evolution of β-propeller assembly and demonstrates the power of our tools.
Iaith wreiddiolSaesneg
Tudalennau (o-i)764-775
Rhif y cyfnodolyn5
Dyddiad ar-lein cynnar7 Maw 2019
Dynodwyr Gwrthrych Digidol (DOIs)
StatwsCyhoeddwyd - 7 Mai 2019
Gweld graff cysylltiadau