High resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica
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ABSTRACT:
SUBMITTER: Ricardo Righetto
PROVIDER: EMPIAR-10389 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica.
Righetto Ricardo D RD Anton Leonie L Adaixo Ricardo R Jakob Roman P RP Zivanov Jasenko J Mahi Mohamed-Ali MA Ringler Philippe P Schwede Torsten T Maier Timm T Stahlberg Henning H
Nature communications 20201009 1
Urease converts urea into ammonia and carbon dioxide and makes urea available as a nitrogen source for all forms of life except animals. In human bacterial pathogens, ureases also aid in the invasion of acidic environments such as the stomach by raising the surrounding pH. Here, we report the structure of urease from the pathogen Yersinia enterocolitica at 2 Å resolution from cryo-electron microscopy. Y. enterocolitica urease is a dodecameric assembly of a trimer of three protein chains, ureA, u ...[more]
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