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dc.contributor.authorNowakowski, Michał
dc.contributor.authorJaremko, Łukasz
dc.contributor.authorWladyka, Benedykt
dc.contributor.authorDubin, Grzegorz
dc.contributor.authorEjchart, Andrzej
dc.contributor.authorMak, Paweł
dc.identifier.citationNowakowski M, Jaremko Ł, Wladyka B, Dubin G, Ejchart A, et al. (2017) Spatial attributes of the four-helix bundle group of bacteriocins – The high-resolution structure of BacSp222 in solution. International Journal of Biological Macromolecules. Available:
dc.description.abstractBacSp222 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.description.sponsorshipThe authors greatly appreciate the valuable advice concerning interpretation of the results provided by Dr. Anna Bujacz. The study was supported in part by a grant (to PM) financed by the National Science Centre (Kraków, Poland) according to decision No. DEC-2013/11/B/NZ6/00409. MN would like to thank the National Science Centre for support with SONATA BIS 2 (2012/07/E/ST4/01386). The Faculty of Biochemistry, Biophysics and Biotechnology of Jagiellonian University in Krakow is a partner of the Leading National Research Center (KNOW) supported by the Ministry of Science and Higher Education (Warszawa, Poland).
dc.publisherElsevier BV
dc.rightsUnder a Creative Commons license
dc.subjectNuclear magnetic resonance
dc.subjectFour-helix bundle bacteriocins
dc.titleSpatial attributes of the four-helix bundle group of bacteriocins – The high-resolution structure of BacSp222 in solution
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.identifier.journalInternational Journal of Biological Macromolecules
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionFaculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Żwirki i Wigury 101, 02-089 Warszawa, Poland
dc.contributor.institutionDepartment of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland
dc.contributor.institutionMałopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7a, 30-387 Kraków, Poland
dc.contributor.institutionDepartment of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland
dc.contributor.institutionInstitute of Biochemistry and Biophysiscs, Polish Academy of Science, Laboratory of Biological NMR, Pawińskiego 5A, 02-106 Warszawa, Poland
kaust.personJaremko, Łukasz

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