{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Guevara T"],"funding":["Ministerstwo Nauki i Szkolnictwa Wyższego","Narodowe Centrum Nauki","Ministerio de Ciencia e Innovación","National Institutes of Health"],"pagination":["18-29"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6949598"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(Pt 1)"],"pubmed_abstract":["<i>Tannerella forsythia</i> is an oral dysbiotic periodontopathogen involved in severe human periodontal disease. As part of its virulence factor armamentarium, at the site of colonization it secretes mirolysin, a metallopeptidase of the unicellular pappalysin family, as a zymogen that is proteolytically auto-activated extracellularly at the Ser54-Arg55 bond. Crystal structures of the catalytically impaired promirolysin point mutant E225A at 1.4 and 1.6 Å revealed that latency is exerted by an N-terminal 34-residue pro-segment that shields the front surface of the 274-residue catalytic domain, thus preventing substrate access. The catalytic domain conforms to the metzincin clan of metallopeptidases and contains a double calcium site, which acts as a calcium switch for activity. The pro-seg"],"journal":["IUCrJ"],"pubmed_title":["Structure-based mechanism of cysteine-switch latency and of catalysis by pappalysin-family metallopeptidases."],"pmcid":["PMC6949598"],"funding_grant_id":["1306/MOB/IV/2015/0"],"pubmed_authors":["Ksiazek M","Guevara T","Gomis-Ruth FX","Potempa J","Rodriguez-Banqueri A"],"additional_accession":[]},"is_claimable":false,"name":"Structure-based mechanism of cysteine-switch latency and of catalysis by pappalysin-family metallopeptidases.","description":"<i>Tannerella forsythia</i> is an oral dysbiotic periodontopathogen involved in severe human periodontal disease. As part of its virulence factor armamentarium, at the site of colonization it secretes mirolysin, a metallopeptidase of the unicellular pappalysin family, as a zymogen that is proteolytically auto-activated extracellularly at the Ser54-Arg55 bond. Crystal structures of the catalytically impaired promirolysin point mutant E225A at 1.4 and 1.6 Å revealed that latency is exerted by an N-terminal 34-residue pro-segment that shields the front surface of the 274-residue catalytic domain, thus preventing substrate access. The catalytic domain conforms to the metzincin clan of metallopeptidases and contains a double calcium site, which acts as a calcium switch for activity. The pro-seg","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jan","modification":"2025-04-26T14:56:23.903Z","creation":"2020-05-22T08:27:24Z"},"accession":"S-EPMC6949598","cross_references":{"pubmed":["31949901"],"doi":["10.1107/S2052252519013848"]}}