{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Turano H"],"funding":["Fundação de Amparo à Pesquisa do Estado de São Paulo"],"pagination":["e00346-20"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7549359"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["202(21)"],"pubmed_abstract":["Multidrug resistance (MDR) is a serious threat to public health, making the development of new antimicrobials an urgent necessity. Pyocins are protein antibiotics produced by <i>Pseudomonas aeruginosa</i> strains to kill closely related cells during intraspecific competition. Here, we report an in-depth biochemical, microbicidal, and structural characterization of a new S-type pyocin, named S8. Initially, we described the domain organization and secondary structure of S8. Subsequently, we observed that a recombinant S8 composed of the killing subunit in complex with the immunity (ImS8) protein killed the strain PAO1. Furthermore, mutation of a highly conserved glutamic acid to alanine (Glu100Ala) completely inhibited this antimicrobial activity. The integrity of the H-N-H motif is probably"],"journal":["Journal of bacteriology"],"pubmed_title":["Molecular Structure and Functional Analysis of Pyocin S8 from Pseudomonas aeruginosa Reveals the Essential Requirement of a Glutamate Residue in the H-N-H Motif for DNase Activity."],"pmcid":["PMC7549359"],"funding_grant_id":["2017/23839-7","2017/09443-3","2013/07937-8"],"pubmed_authors":["Domingos RM","Netto LES","Lincopan N","Turano H","Gomes F","Garratt RC","Degenhardt MFS","Oliveira CLP"],"additional_accession":[]},"is_claimable":false,"name":"Molecular Structure and Functional Analysis of Pyocin S8 from Pseudomonas aeruginosa Reveals the Essential Requirement of a Glutamate Residue in the H-N-H Motif for DNase Activity.","description":"Multidrug resistance (MDR) is a serious threat to public health, making the development of new antimicrobials an urgent necessity. Pyocins are protein antibiotics produced by <i>Pseudomonas aeruginosa</i> strains to kill closely related cells during intraspecific competition. Here, we report an in-depth biochemical, microbicidal, and structural characterization of a new S-type pyocin, named S8. Initially, we described the domain organization and secondary structure of S8. Subsequently, we observed that a recombinant S8 composed of the killing subunit in complex with the immunity (ImS8) protein killed the strain PAO1. Furthermore, mutation of a highly conserved glutamic acid to alanine (Glu100Ala) completely inhibited this antimicrobial activity. The integrity of the H-N-H motif is probably","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Oct","modification":"2026-05-01T16:31:15.685Z","creation":"2022-02-09T12:51:59.514Z"},"accession":"S-EPMC7549359","cross_references":{"pubmed":["32817098"],"doi":["10.1128/JB.00346-20","10.1128/jb.00346-20"]}}