NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold

Abstract In addition to multiple virulence factors, Bacillus cereus a pathogen that causes food poisoning and life-threatening wound infections, secretes the pore-forming toxin hemolysin II (HlyII). The HlyII toxin has a unique 94 amino acid C-terminal domain (HlyIIC). HlyIIC exhibits splitting of N...

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Autores principales:	Anne R. Kaplan, Katherine Kaus, Swastik De, Rich Olson, Andrei T. Alexandrescu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0ba821a0456742d090fc2ca6e2423836
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spelling	oai:doaj.org-article:0ba821a0456742d090fc2ca6e24238362021-12-02T12:32:00ZNMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold10.1038/s41598-017-02917-42045-2322https://doaj.org/article/0ba821a0456742d090fc2ca6e24238362017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02917-4https://doaj.org/toc/2045-2322Abstract In addition to multiple virulence factors, Bacillus cereus a pathogen that causes food poisoning and life-threatening wound infections, secretes the pore-forming toxin hemolysin II (HlyII). The HlyII toxin has a unique 94 amino acid C-terminal domain (HlyIIC). HlyIIC exhibits splitting of NMR resonances due to cis/trans isomerization of a single proline near the C-terminus. To overcome heterogeneity, we solved the structure of P405M-HlyIIC, a mutant that exclusively stabilizes the trans state. The NMR structure of HlyIIC reveals a novel fold, consisting of two subdomains αA-β1-β2 and β3-β4-αB-β5, that come together in a barrel-like structure. The barrel core is fastened by three layers of hydrophobic residues. The barrel end opposite the HlyIIC-core has a positively charged surface, that by binding negatively charged moieties on cellular membranes, may play a role in target-cell surface recognition or stabilization of the heptameric pore complex. In the WT domain, dynamic flexibility occurs at the N-terminus and the first α-helix that connects the HlyIIC domain to the HlyII-core structure. In the destabilizing P405M mutant, increased flexibility is evident throughout the first subdomain, suggesting that the HlyIIC structure may have arisen through gene fusion.Anne R. KaplanKatherine KausSwastik DeRich OlsonAndrei T. AlexandrescuNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anne R. Kaplan Katherine Kaus Swastik De Rich Olson Andrei T. Alexandrescu NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold
description	Abstract In addition to multiple virulence factors, Bacillus cereus a pathogen that causes food poisoning and life-threatening wound infections, secretes the pore-forming toxin hemolysin II (HlyII). The HlyII toxin has a unique 94 amino acid C-terminal domain (HlyIIC). HlyIIC exhibits splitting of NMR resonances due to cis/trans isomerization of a single proline near the C-terminus. To overcome heterogeneity, we solved the structure of P405M-HlyIIC, a mutant that exclusively stabilizes the trans state. The NMR structure of HlyIIC reveals a novel fold, consisting of two subdomains αA-β1-β2 and β3-β4-αB-β5, that come together in a barrel-like structure. The barrel core is fastened by three layers of hydrophobic residues. The barrel end opposite the HlyIIC-core has a positively charged surface, that by binding negatively charged moieties on cellular membranes, may play a role in target-cell surface recognition or stabilization of the heptameric pore complex. In the WT domain, dynamic flexibility occurs at the N-terminus and the first α-helix that connects the HlyIIC domain to the HlyII-core structure. In the destabilizing P405M mutant, increased flexibility is evident throughout the first subdomain, suggesting that the HlyIIC structure may have arisen through gene fusion.
format	article
author	Anne R. Kaplan Katherine Kaus Swastik De Rich Olson Andrei T. Alexandrescu
author_facet	Anne R. Kaplan Katherine Kaus Swastik De Rich Olson Andrei T. Alexandrescu
author_sort	Anne R. Kaplan
title	NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold
title_short	NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold
title_full	NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold
title_fullStr	NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold
title_full_unstemmed	NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold
title_sort	nmr structure of the bacillus cereus hemolysin ii c-terminal domain reveals a novel fold
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/0ba821a0456742d090fc2ca6e2423836
work_keys_str_mv	AT annerkaplan nmrstructureofthebacilluscereushemolysiniicterminaldomainrevealsanovelfold AT katherinekaus nmrstructureofthebacilluscereushemolysiniicterminaldomainrevealsanovelfold AT swastikde nmrstructureofthebacilluscereushemolysiniicterminaldomainrevealsanovelfold AT richolson nmrstructureofthebacilluscereushemolysiniicterminaldomainrevealsanovelfold AT andreitalexandrescu nmrstructureofthebacilluscereushemolysiniicterminaldomainrevealsanovelfold
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NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold

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