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7NYI

BacSp222 bacteriocin: succinyl-K20 form

Summary for 7NYI
Entry DOI10.2210/pdb7nyi/pdb
NMR InformationBMRB: 34614
DescriptorBacteriocin BacSp222 (1 entity in total)
Functional Keywordspeptide bacteriocin, succinylation, antimicrobial protein
Biological sourceStaphylococcus pseudintermedius
Total number of polymer chains1
Total formula weight6028.94
Authors
Nowakowski, M.,Mak, P.,Smialek, J. (deposition date: 2021-03-22, release date: 2021-07-07, Last modification date: 2025-04-09)
Primary citationSmialek, J.,Nowakowski, M.,Bzowska, M.,Bochenska, O.,Wlizlo, A.,Kozik, A.,Dubin, G.,Mak, P.
Structure, Biosynthesis, and Biological Activity of Succinylated Forms of Bacteriocin BacSp222.
Int J Mol Sci, 22:-, 2021
Cited by
PubMed Abstract: BacSp222 is a multifunctional peptide produced by 222. This 50-amino acid long peptide belongs to subclass IId of bacteriocins and forms a four-helix bundle molecule. In addition to bactericidal functions, BacSp222 possesses also features of a virulence factor, manifested in immunomodulatory and cytotoxic activities toward eukaryotic cells. In the present study, we demonstrate that BacSp222 is produced in several post-translationally modified forms, succinylated at the ε-amino group of lysine residues. Such modifications have not been previously described for any bacteriocins. NMR and circular dichroism spectroscopy studies have shown that the modifications do not alter the spatial structure of the peptide. At the same time, succinylation significantly diminishes its bactericidal and cytotoxic potential. We demonstrate that the modification of the bacteriocin is an effect of non-enzymatic reaction with a highly reactive intracellular metabolite, i.e., succinyl-coenzyme A. The production of succinylated forms of the bacteriocin depends on environmental factors and on the access of bacteria to nutrients. Our study indicates that the production of succinylated forms of bacteriocin occurs in response to the changing environment, protects producer cells against the autotoxicity of the excreted peptide, and limits the pathogenicity of the strain.
PubMed: 34200765
DOI: 10.3390/ijms22126256
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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