<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Turano H</submitter><funding>Fundação de Amparo à Pesquisa do Estado de São Paulo</funding><pagination>e00346-20</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7549359</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>202(21)</volume><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 &lt;i>Pseudomonas aeruginosa&lt;/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</pubmed_abstract><journal>Journal of bacteriology</journal><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.</pubmed_title><pmcid>PMC7549359</pmcid><funding_grant_id>2017/23839-7</funding_grant_id><funding_grant_id>2017/09443-3</funding_grant_id><funding_grant_id>2013/07937-8</funding_grant_id><pubmed_authors>Domingos RM</pubmed_authors><pubmed_authors>Netto LES</pubmed_authors><pubmed_authors>Lincopan N</pubmed_authors><pubmed_authors>Turano H</pubmed_authors><pubmed_authors>Gomes F</pubmed_authors><pubmed_authors>Garratt RC</pubmed_authors><pubmed_authors>Degenhardt MFS</pubmed_authors><pubmed_authors>Oliveira CLP</pubmed_authors></additional><is_claimable>false</is_claimable><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.</name><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 &lt;i>Pseudomonas aeruginosa&lt;/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</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Oct</publication><modification>2026-05-01T16:31:15.685Z</modification><creation>2022-02-09T12:51:59.514Z</creation></dates><accession>S-EPMC7549359</accession><cross_references><pubmed>32817098</pubmed><doi>10.1128/JB.00346-20</doi><doi>10.1128/jb.00346-20</doi></cross_references></HashMap>