Abstract
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.
Highlights
Urease converts urea into ammonia and carbon dioxide and makes urea available as a nitrogen source for all forms of life except animals
The dodecameric holoenzyme structure of ureases might aid in stabilizing the protein at acidic pH, and in combination with 12 active sites producing ammonia enables the formation of a pH-neutralizing microenvironment around the assembly22
The positions of the side chains and the Ni2+ ions in the active site are very similar to the Y. enterocolitica urease structure with a root mean square deviations (RMSDs) of 0.270 Å (Supplementary Table S5)
Summary
Urease converts urea into ammonia and carbon dioxide and makes urea available as a nitrogen source for all forms of life except animals. The urease of the opportunistic pathogen Klebsiella aerogenes10 assembles into a heterotrimer of three proteins ureA, ureB, and ureC, which in turn oligomerizes into a trimer ([αβγ]3 C3)11 (Fig. 1b, c).
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
