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TitleHigh-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 5101, Year 2020
Publish dateOct 9, 2020
AuthorsRicardo D Righetto / Leonie Anton / Ricardo Adaixo / Roman P Jakob / Jasenko Zivanov / Mohamed-Ali Mahi / Philippe Ringler / Torsten Schwede / Timm Maier / Henning Stahlberg /
PubMed AbstractUrease 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 ...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, ureB and ureC. The high data quality enables detailed visualization of the urease bimetal active site and of the impact of radiation damage. The obtained structure is of sufficient quality to support drug development efforts.
External linksNat Commun / PubMed:33037208
MethodsEM (single particle)
Resolution1.98 Å
Structure data

EMDB-10835, PDB-6yl3:
High resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica
Method: EM (single particle) / Resolution: 1.98 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION / Nickel

ChemComp-HOH:
WATER / Water

Source
  • yersinia enterocolitica w22703 (bacteria)
KeywordsMETAL BINDING PROTEIN / Urease / enzyme / nickel / metalloenzyme / pathogen

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