Structural Analysis of Glutamine Synthetase from Helicobacter pylori

Abstract Glutamine synthetase (GS) is an enzyme that regulates nitrogen metabolism and synthesizes glutamine via glutamate, ATP, and ammonia. GS is a homo-oligomeric protein of eight, ten, or twelve subunits, and each subunit-subunit interface has its own active site. GS can be divided into GS I, GS...

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Autores principales:	Hyun Kyu Joo, Young Woo Park, Young Yoon Jang, Jae Young Lee
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/435ce78f2e454f3ab377e50ac2921377
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spelling	oai:doaj.org-article:435ce78f2e454f3ab377e50ac29213772021-12-02T15:07:46ZStructural Analysis of Glutamine Synthetase from Helicobacter pylori10.1038/s41598-018-30191-52045-2322https://doaj.org/article/435ce78f2e454f3ab377e50ac29213772018-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-30191-5https://doaj.org/toc/2045-2322Abstract Glutamine synthetase (GS) is an enzyme that regulates nitrogen metabolism and synthesizes glutamine via glutamate, ATP, and ammonia. GS is a homo-oligomeric protein of eight, ten, or twelve subunits, and each subunit-subunit interface has its own active site. GS can be divided into GS I, GS II, and GS III. GS I and GS III form dodecamer in bacteria and archaea, whereas GS II form decamer in eukaryotes. GS I can be further subdivided into GS I-α and GS I-β according to its sequence and regulatory mechanism. GS is an essential protein for the survival of Helicobacter pylori which its infection could promote gastroduodenal diseases. Here, we determined the crystal structures of the GS from H. pylori (Hpy GS) in its apo- and substrate-bound forms at 2.8 Å and 2.9 Å resolution, respectively. Hpy GS formed a dodecamer composed of two hexameric rings stacked face-to-face. Hpy GS, which belongs to GS I, cannot be clearly classified as either GS I-α or GS I-β based on its sequence and regulatory mechanism. In this study, we propose that Hpy GS could be classified as a new GS-I subfamily and provide structural information on the apo- and substrate-bound forms of the protein.Hyun Kyu JooYoung Woo ParkYoung Yoon JangJae Young LeeNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-8 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hyun Kyu Joo Young Woo Park Young Yoon Jang Jae Young Lee Structural Analysis of Glutamine Synthetase from Helicobacter pylori
description	Abstract Glutamine synthetase (GS) is an enzyme that regulates nitrogen metabolism and synthesizes glutamine via glutamate, ATP, and ammonia. GS is a homo-oligomeric protein of eight, ten, or twelve subunits, and each subunit-subunit interface has its own active site. GS can be divided into GS I, GS II, and GS III. GS I and GS III form dodecamer in bacteria and archaea, whereas GS II form decamer in eukaryotes. GS I can be further subdivided into GS I-α and GS I-β according to its sequence and regulatory mechanism. GS is an essential protein for the survival of Helicobacter pylori which its infection could promote gastroduodenal diseases. Here, we determined the crystal structures of the GS from H. pylori (Hpy GS) in its apo- and substrate-bound forms at 2.8 Å and 2.9 Å resolution, respectively. Hpy GS formed a dodecamer composed of two hexameric rings stacked face-to-face. Hpy GS, which belongs to GS I, cannot be clearly classified as either GS I-α or GS I-β based on its sequence and regulatory mechanism. In this study, we propose that Hpy GS could be classified as a new GS-I subfamily and provide structural information on the apo- and substrate-bound forms of the protein.
format	article
author	Hyun Kyu Joo Young Woo Park Young Yoon Jang Jae Young Lee
author_facet	Hyun Kyu Joo Young Woo Park Young Yoon Jang Jae Young Lee
author_sort	Hyun Kyu Joo
title	Structural Analysis of Glutamine Synthetase from Helicobacter pylori
title_short	Structural Analysis of Glutamine Synthetase from Helicobacter pylori
title_full	Structural Analysis of Glutamine Synthetase from Helicobacter pylori
title_fullStr	Structural Analysis of Glutamine Synthetase from Helicobacter pylori
title_full_unstemmed	Structural Analysis of Glutamine Synthetase from Helicobacter pylori
title_sort	structural analysis of glutamine synthetase from helicobacter pylori
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/435ce78f2e454f3ab377e50ac2921377
work_keys_str_mv	AT hyunkyujoo structuralanalysisofglutaminesynthetasefromhelicobacterpylori AT youngwoopark structuralanalysisofglutaminesynthetasefromhelicobacterpylori AT youngyoonjang structuralanalysisofglutaminesynthetasefromhelicobacterpylori AT jaeyounglee structuralanalysisofglutaminesynthetasefromhelicobacterpylori
_version_	1718388380348186624

Structural Analysis of Glutamine Synthetase from Helicobacter pylori

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