Spatial attributes of the four-helix bundle group of bacteriocins - The high-resolution structure of BacSp222 in solution
| Autor: | Benedykt Wladyka, Łukasz Jaremko, Andrzej Ejchart, Michał Nowakowski, Grzegorz Dubin, Paweł Mak |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Models Molecular Staphylococcus pseudintermedius Proton Magnetic Resonance Spectroscopy Peptide BacSp222 Biology Biochemistry Protein Structure Secondary 03 medical and health sciences Bacteriocin Bacteriocins Structural Biology Amino Acid Sequence four-helix bundle bacteriocins Molecular Biology Peptide sequence chemistry.chemical_classification Helix bundle Strain (chemistry) Tryptophan General Medicine biology.organism_classification Solutions nuclear magnetic resonance 030104 developmental biology chemistry Structural Homology Protein Thermodynamics Bacteria |
| Zdroj: | International journal of biological macromolecules. 107 |
| ISSN: | 1879-0003 |
| Popis: | BacSp222 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. |
| Databáze: | OpenAIRE |
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