6YL3

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

This is a non-PDB format compatible entry.

Summary for 6YL3

• Entry DOI: 10.2210/pdb6yl3/pdb
• EMDB information: 10835
• Descriptor: Urease subunit gamma, Urease subunit beta, Urease subunit alpha, ... (5 entities in total)
• Functional Keywords: urease, enzyme, nickel, metalloenzyme, pathogen, metal binding protein
• Biological source: Yersinia enterocolitica W22703; More
• Total number of polymer chains: 36
• Total formula weight: 1042168.79

Authors

Righetto, R.D.,Anton, L.,Adaixo, R.,Jakob, R.,Zivanov, J.,Mahi, M.A.,Ringler, P.,Schwede, T.,Maier, T.,Stahlberg, H. (deposition date: 2020-04-06, release date: 2020-05-06, Last modification date: 2025-04-09)

Primary citation

Righetto, R.D.,Anton, L.,Adaixo, R.,Jakob, R.P.,Zivanov, J.,Mahi, M.A.,Ringler, P.,Schwede, T.,Maier, T.,Stahlberg, H.
High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica.
Nat Commun, 11:5101-5101, 2020

PubMed 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.

PubMed: 33037208
DOI: 10.1038/s41467-020-18870-2

Experimental method

ELECTRON MICROSCOPY (1.98 Å)