7NS1

S. aureus pepG1 NMR solution structure

Summary for 7NS1

• Entry DOI: 10.2210/pdb7ns1/pdb
• NMR Information: BMRB: 50767
• Descriptor: Snterotoxin A (1 entity in total)
• Functional Keywords: pepg1, sprg1 product, s. aureus, toxin, solution structure
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 3465.37

Authors

Nonin-Lecomte, S.,fermon, L.,Felden, B.,Pinel-Marie, M.L. (deposition date: 2021-03-05, release date: 2021-07-21, Last modification date: 2024-06-19)

Primary citation

Nonin-Lecomte, S.,Fermon, L.,Felden, B.,Pinel-Marie, M.L.
Bacterial Type I Toxins: Folding and Membrane Interactions.
Toxins, 13:-, 2021

PubMed Abstract: Bacterial type I toxin-antitoxin systems are two-component genetic modules that encode a stable toxic protein whose ectopic overexpression can lead to growth arrest or cell death, and an unstable RNA antitoxin that inhibits toxin translation during growth. These systems are widely spread among bacterial species. Type I antitoxins are - or -encoded antisense small RNAs that interact with toxin-encoding mRNAs by pairing, thereby inhibiting toxin mRNA translation and/or inducing its degradation. Under environmental stress conditions, the up-regulation of the toxin and/or the antitoxin degradation by specific RNases promote toxin translation. Most type I toxins are small hydrophobic peptides with a predicted α-helical transmembrane domain that induces membrane depolarization and/or permeabilization followed by a decrease of intracellular ATP, leading to plasmid maintenance, growth adaptation to environmental stresses, or persister cell formation. In this review, we describe the current state of the art on the folding and the membrane interactions of these membrane-associated type I toxins from either Gram-negative or Gram-positive bacteria and establish a chronology of their toxic effects on the bacterial cell. This review also includes novel structural results obtained by NMR concerning the -encoded membrane peptides that belong to the /SprF1 type I TA system expressed in and discusses the putative membrane interactions allowing the lysis of competing bacteria and host cells.

PubMed: 34357962
DOI: 10.3390/toxins13070490

Experimental method

SOLUTION NMR