Back to Search Start Over

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

Authors :
Ricardo D. Righetto
Leonie Anton
Ricardo Adaixo
Roman P. Jakob
Jasenko Zivanov
Mohamed-Ali Mahi
Philippe Ringler
Torsten Schwede
Timm Maier
Henning Stahlberg
Source :
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
Publication Year :
2020
Publisher :
Nature Portfolio, 2020.

Abstract

Urease is a nickel enzyme responsible for catalyzing the conversion of urea into ammonia and carbon dioxide. Here the authors report a high resolution cryo-EM structure of urease from the bacterial pathogen Yersinia enterocolitica, providing a detailed visualization of the urease bimetal active site and a basis for drug development.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
11
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.3061b5e260314c16bdfa321e2acc5397
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-020-18870-2