5LWC
NMR solution structure of bacteriocin BacSp222 from Staphylococcus pseudintermedius 222
Summary for 5LWC
| Entry DOI | 10.2210/pdb5lwc/pdb |
| NMR Information | BMRB: 34044 |
| Descriptor | Bacteriocin BacSp222 (1 entity in total) |
| Functional Keywords | bacteriocin, structure from molmol, antimicrobial protein |
| Biological source | Staphylococcus pseudintermedius |
| Total number of polymer chains | 1 |
| Total formula weight | 5929.88 |
| Authors | Nowakowski, M.E.,Ejchart, A.O.,Jaremko, L.,Wladyka, B.,Mak, P. (deposition date: 2016-09-15, release date: 2017-10-25, Last modification date: 2024-10-23) |
| Primary citation | Nowakowski, M.,Jaremko, L.,Wladyka, B.,Dubin, G.,Ejchart, A.,Mak, P. Spatial attributes of the four-helix bundle group of bacteriocins - The high-resolution structure of BacSp222 in solution. Int.J.Biol.Macromol., 107:2715-2724, 2018 Cited by PubMed Abstract: 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 C- and N-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. PubMed: 29107139DOI: 10.1016/j.ijbiomac.2017.10.158 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
