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Spatial attributes of the four-helix bundle group of bacteriocins - The high-resolution structure of BacSp222 in solution

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cris.lastimport.scopus2024-02-12T20:24:31Z
dc.abstract.enBacSp222 is a multifunctional bacteriocin produced by Staphylococcus pseudintermedius strain 222, an opportunistic pathogen of domestic animals. At micromolar concentrations, BacSp222 kills Gram-positive bacteria and is cytotoxic toward mammalian cells, while at nanomolar doses, it acts as an immunomodulatory factor, enhancing nitric oxide release in macrophage-like cell lines. The bacteriocin is a cationic, N-terminally formylated, 50-amino-acid-long linear peptide that is rich in tryptophan residues. In this study, the solution structure of BacSp222 was determined and compared to the currently known structures of similar bacteriocins. BacSp222 was isolated from a liquid culture medium in a uniformly 13C- and 15N-labeled form, and NMR data were collected. The structure was calculated based on NMR-derived constraints and consists of a rigid and tightly packed globular bundle of four alpha-helices separated by three short turns. Although the amino acid sequence of BacSp222 has no significant similarity to any known peptide or protein, a 3D structure similarity search indicates a close relation to other four-helix bundle-motif bacteriocins, such as aureocin A53, lacticin Q and enterocins 7A/7B. Assuming similar functions, biology, structure and physicochemical properties, we propose to distinguish the four-helix bundle bacteriocins as a new Type A in subclass IId of bacteriocins, containing linear, non-pediocin-like peptides.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorDubin, Grzegorz
dc.contributor.authorEjchart, Andrzej
dc.contributor.authorMak, Paweł
dc.contributor.authorNowakowski, Michał
dc.contributor.authorJaremko, Łukasz
dc.contributor.authorWładyka, Benedykt
dc.date.accessioned2024-01-26T07:54:03Z
dc.date.available2024-01-26T07:54:03Z
dc.date.issued2018
dc.description.accesstimeAT_PUBLICATION
dc.description.financeNie dotyczy
dc.description.versionFINAL_PUBLISHED
dc.description.volume107
dc.identifier.doi10.1016/J.IJBIOMAC.2017.10.158
dc.identifier.issn0141-8130
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/120277
dc.identifier.weblinkhttps://www.sciencedirect.com/science/article/pii/S0141813017330635?via%3Dihub
dc.languageeng
dc.pbn.affiliationchemical sciences
dc.relation.ispartofInternational Journal of Biological Macromolecules
dc.relation.pages2715-2724
dc.rightsCC-BY-NC-ND
dc.sciencecloudnosend
dc.subject.enBacSp222
dc.subject.enFour-helix bundle bacteriocins
dc.subject.enNuclear magnetic resonance
dc.titleSpatial attributes of the four-helix bundle group of bacteriocins - The high-resolution structure of BacSp222 in solution
dc.typeJournalArticle
dspace.entity.typePublication