High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica.
Details
Serval ID
serval:BIB_62085E6BB082
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica.
Journal
Nature communications
ISSN
2041-1723 (Electronic)
ISSN-L
2041-1723
Publication state
Published
Issued date
09/10/2020
Peer-reviewed
Oui
Volume
11
Number
1
Pages
5101
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Publication Status: epublish
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.
Keywords
Bacterial Proteins/chemistry, Bacterial Proteins/metabolism, Catalytic Domain, Cryoelectron Microscopy, Lysine/metabolism, Models, Molecular, Nickel/chemistry, Nickel/metabolism, Protein Conformation, Protein Domains, Urease/chemistry, Urease/metabolism, Water/chemistry, Yersinia enterocolitica/enzymology
Pubmed
Web of science
Open Access
Yes
Create date
09/06/2023 16:02
Last modification date
08/07/2023 6:50