Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae

Abstract Cyclic diguanylate monophosphate (c-di-GMP) is a second messenger involved in bacterial signal transduction and produced by diguanylate cyclases (DGCs) generally containing highly variable periplasmic signal-recognition domains. CdgH is a DGC enzyme that regulates rugosity associated phenot...

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Autores principales:	Min Xu, Yi-Zhi Wang, Xiu-An Yang, Tao Jiang, Wei Xie
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/40ea0cceb9274de889569ede9a1a2bf8
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spelling	oai:doaj.org-article:40ea0cceb9274de889569ede9a1a2bf82021-12-02T15:06:15ZStructural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae10.1038/s41598-017-01989-62045-2322https://doaj.org/article/40ea0cceb9274de889569ede9a1a2bf82017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01989-6https://doaj.org/toc/2045-2322Abstract Cyclic diguanylate monophosphate (c-di-GMP) is a second messenger involved in bacterial signal transduction and produced by diguanylate cyclases (DGCs) generally containing highly variable periplasmic signal-recognition domains. CdgH is a DGC enzyme that regulates rugosity associated phenotypes in Vibrio cholerae. CdgH has two N-terminal tandem periplasmic substrate-binding (PBPb) domains for its signal recognition; however, the role of the tandem PBPb domains remains unclear. Here, we reported the crystal structure of the periplasmic portion of CdgH, which indicated that both tandem PBPb domains consist of typical interlobe ligand-binding architecture. Unexpectedly, the PBPb-I domain binds an L-arginine which apparently has been co-purified from the E. coli expression system, whereas the PBPb-II domain is in an unliganded open state. Structural comparison with other amino acid-binding proteins indicated that despite similar ligand-binding pockets, the PBPb-I domain possesses two ligand-binding residues (E122 and Y148) not conserved in homologs and involved in hydrophilic and hydrophobic interactions with L-arginine. Isothermal titration calorimetry indicated that the PBPb-I is primarily an L-arginine/L-lysine/L-ornithine-binding domain, whereas the PBPb-II domain exhibits a preference for L-glutamine and L-histidine. Remarkably, we found that the periplasmic portion of CdgH forms a stable dimer in solution and L-arginine binding would cause conformational changes of the dimer.Min XuYi-Zhi WangXiu-An YangTao JiangWei XieNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Min Xu Yi-Zhi Wang Xiu-An Yang Tao Jiang Wei Xie Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae
description	Abstract Cyclic diguanylate monophosphate (c-di-GMP) is a second messenger involved in bacterial signal transduction and produced by diguanylate cyclases (DGCs) generally containing highly variable periplasmic signal-recognition domains. CdgH is a DGC enzyme that regulates rugosity associated phenotypes in Vibrio cholerae. CdgH has two N-terminal tandem periplasmic substrate-binding (PBPb) domains for its signal recognition; however, the role of the tandem PBPb domains remains unclear. Here, we reported the crystal structure of the periplasmic portion of CdgH, which indicated that both tandem PBPb domains consist of typical interlobe ligand-binding architecture. Unexpectedly, the PBPb-I domain binds an L-arginine which apparently has been co-purified from the E. coli expression system, whereas the PBPb-II domain is in an unliganded open state. Structural comparison with other amino acid-binding proteins indicated that despite similar ligand-binding pockets, the PBPb-I domain possesses two ligand-binding residues (E122 and Y148) not conserved in homologs and involved in hydrophilic and hydrophobic interactions with L-arginine. Isothermal titration calorimetry indicated that the PBPb-I is primarily an L-arginine/L-lysine/L-ornithine-binding domain, whereas the PBPb-II domain exhibits a preference for L-glutamine and L-histidine. Remarkably, we found that the periplasmic portion of CdgH forms a stable dimer in solution and L-arginine binding would cause conformational changes of the dimer.
format	article
author	Min Xu Yi-Zhi Wang Xiu-An Yang Tao Jiang Wei Xie
author_facet	Min Xu Yi-Zhi Wang Xiu-An Yang Tao Jiang Wei Xie
author_sort	Min Xu
title	Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae
title_short	Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae
title_full	Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae
title_fullStr	Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae
title_full_unstemmed	Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae
title_sort	structural studies of the periplasmic portion of the diguanylate cyclase cdgh from vibrio cholerae
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/40ea0cceb9274de889569ede9a1a2bf8
work_keys_str_mv	AT minxu structuralstudiesoftheperiplasmicportionofthediguanylatecyclasecdghfromvibriocholerae AT yizhiwang structuralstudiesoftheperiplasmicportionofthediguanylatecyclasecdghfromvibriocholerae AT xiuanyang structuralstudiesoftheperiplasmicportionofthediguanylatecyclasecdghfromvibriocholerae AT taojiang structuralstudiesoftheperiplasmicportionofthediguanylatecyclasecdghfromvibriocholerae AT weixie structuralstudiesoftheperiplasmicportionofthediguanylatecyclasecdghfromvibriocholerae
_version_	1718388507108442112

Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae

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