The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity

Abstract Previously, we reported the isolation of a quorum quenching protein (QQ), designated GqqA, from Komagataeibacter europaeus CECT 8546 that is highly homologous to prephenate dehydratases (PDT) (Valera et al. in Microb Cell Fact 15, 88. https://doi.org/10.1186/s12934-016-0482-y , 2016). GqqA...

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Autores principales:	Nadine Werner, Katrin Petersen, Christel Vollstedt, Pablo Perez Garcia, Jennifer Chow, Manuel Ferrer, Laura Fernandez-Lopez, Sven Falke, Markus Perbandt, Winfried Hinrichs, Christian Betzel, Wolfgang R. Streit
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/54f7a0561304488884a0ca633d03a700
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spelling	oai:doaj.org-article:54f7a0561304488884a0ca633d03a7002021-12-02T14:58:19ZThe Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity10.1038/s41598-021-91536-12045-2322https://doaj.org/article/54f7a0561304488884a0ca633d03a7002021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-91536-1https://doaj.org/toc/2045-2322Abstract Previously, we reported the isolation of a quorum quenching protein (QQ), designated GqqA, from Komagataeibacter europaeus CECT 8546 that is highly homologous to prephenate dehydratases (PDT) (Valera et al. in Microb Cell Fact 15, 88. https://doi.org/10.1186/s12934-016-0482-y , 2016). GqqA strongly interfered with N-acyl-homoserine lactone (AHL) quorum sensing signals from Gram-negative bacteria and affected biofilm formation in its native host strain Komagataeibacter europaeus. Here we present and discuss data identifying GqqA as a novel acylase. ESI–MS–MS data showed unambiguously that GqqA hydrolyzes the amide bond of the acyl side-chain of AHL molecules, but not the lactone ring. Consistent with this observation the protein sequence does not carry a conserved Zn2+ binding motif, known to be essential for metal-dependent lactonases, but in fact harboring the typical periplasmatic binding protein domain (PBP domain), acting as catalytic domain. We report structural details for the native structure at 2.5 Å resolution and for a truncated GqqA structure at 1.7 Å. The structures obtained highlight that GqqA acts as a dimer and complementary docking studies indicate that the lactone ring of the substrate binds within a cleft of the PBP domain and interacts with polar residues Y16, S17 and T174. The biochemical and phylogenetic analyses imply that GqqA represents the first member of a novel type of QQ family enzymes.Nadine WernerKatrin PetersenChristel VollstedtPablo Perez GarciaJennifer ChowManuel FerrerLaura Fernandez-LopezSven FalkeMarkus PerbandtWinfried HinrichsChristian BetzelWolfgang R. StreitNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nadine Werner Katrin Petersen Christel Vollstedt Pablo Perez Garcia Jennifer Chow Manuel Ferrer Laura Fernandez-Lopez Sven Falke Markus Perbandt Winfried Hinrichs Christian Betzel Wolfgang R. Streit The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity
description	Abstract Previously, we reported the isolation of a quorum quenching protein (QQ), designated GqqA, from Komagataeibacter europaeus CECT 8546 that is highly homologous to prephenate dehydratases (PDT) (Valera et al. in Microb Cell Fact 15, 88. https://doi.org/10.1186/s12934-016-0482-y , 2016). GqqA strongly interfered with N-acyl-homoserine lactone (AHL) quorum sensing signals from Gram-negative bacteria and affected biofilm formation in its native host strain Komagataeibacter europaeus. Here we present and discuss data identifying GqqA as a novel acylase. ESI–MS–MS data showed unambiguously that GqqA hydrolyzes the amide bond of the acyl side-chain of AHL molecules, but not the lactone ring. Consistent with this observation the protein sequence does not carry a conserved Zn2+ binding motif, known to be essential for metal-dependent lactonases, but in fact harboring the typical periplasmatic binding protein domain (PBP domain), acting as catalytic domain. We report structural details for the native structure at 2.5 Å resolution and for a truncated GqqA structure at 1.7 Å. The structures obtained highlight that GqqA acts as a dimer and complementary docking studies indicate that the lactone ring of the substrate binds within a cleft of the PBP domain and interacts with polar residues Y16, S17 and T174. The biochemical and phylogenetic analyses imply that GqqA represents the first member of a novel type of QQ family enzymes.
format	article
author	Nadine Werner Katrin Petersen Christel Vollstedt Pablo Perez Garcia Jennifer Chow Manuel Ferrer Laura Fernandez-Lopez Sven Falke Markus Perbandt Winfried Hinrichs Christian Betzel Wolfgang R. Streit
author_facet	Nadine Werner Katrin Petersen Christel Vollstedt Pablo Perez Garcia Jennifer Chow Manuel Ferrer Laura Fernandez-Lopez Sven Falke Markus Perbandt Winfried Hinrichs Christian Betzel Wolfgang R. Streit
author_sort	Nadine Werner
title	The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity
title_short	The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity
title_full	The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity
title_fullStr	The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity
title_full_unstemmed	The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity
title_sort	komagataeibacter europaeus gqqa is the prototype of a novel bifunctional n-acyl-homoserine lactone acylase with prephenate dehydratase activity
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/54f7a0561304488884a0ca633d03a700
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The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity

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