Nature Communications (Oct 2020)

High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica

  • Ricardo D. Righetto,
  • Leonie Anton,
  • Ricardo Adaixo,
  • Roman P. Jakob,
  • Jasenko Zivanov,
  • Mohamed-Ali Mahi,
  • Philippe Ringler,
  • Torsten Schwede,
  • Timm Maier,
  • Henning Stahlberg

DOI
https://doi.org/10.1038/s41467-020-18870-2
Journal volume & issue
Vol. 11, no. 1
pp. 1 – 10

Abstract

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Urease is a nickel enzyme responsible for catalyzing the conversion of urea into ammonia and carbon dioxide. Here the authors report a high resolution cryo-EM structure of urease from the bacterial pathogen Yersinia enterocolitica, providing a detailed visualization of the urease bimetal active site and a basis for drug development.