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

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...

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Autores principales:	Ricardo D. Righetto, Leonie Anton, Ricardo Adaixo, Roman P. Jakob, Jasenko Zivanov, Mohamed-Ali Mahi, Philippe Ringler, Torsten Schwede, Timm Maier, Henning Stahlberg
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3061b5e260314c16bdfa321e2acc5397
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spelling	oai:doaj.org-article:3061b5e260314c16bdfa321e2acc53972021-12-02T17:13:19ZHigh-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica10.1038/s41467-020-18870-22041-1723https://doaj.org/article/3061b5e260314c16bdfa321e2acc53972020-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-18870-2https://doaj.org/toc/2041-1723Urease 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.Ricardo D. RighettoLeonie AntonRicardo AdaixoRoman P. JakobJasenko ZivanovMohamed-Ali MahiPhilippe RinglerTorsten SchwedeTimm MaierHenning StahlbergNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ricardo D. Righetto Leonie Anton Ricardo Adaixo Roman P. Jakob Jasenko Zivanov Mohamed-Ali Mahi Philippe Ringler Torsten Schwede Timm Maier Henning Stahlberg High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica
description	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.
format	article
author	Ricardo D. Righetto Leonie Anton Ricardo Adaixo Roman P. Jakob Jasenko Zivanov Mohamed-Ali Mahi Philippe Ringler Torsten Schwede Timm Maier Henning Stahlberg
author_facet	Ricardo D. Righetto Leonie Anton Ricardo Adaixo Roman P. Jakob Jasenko Zivanov Mohamed-Ali Mahi Philippe Ringler Torsten Schwede Timm Maier Henning Stahlberg
author_sort	Ricardo D. Righetto
title	High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica
title_short	High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica
title_full	High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica
title_fullStr	High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica
title_full_unstemmed	High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica
title_sort	high-resolution cryo-em structure of urease from the pathogen yersinia enterocolitica
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/3061b5e260314c16bdfa321e2acc5397
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High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica

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