{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Goulas T"],"funding":["European Commission FP7"],"pagination":["1856-61"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3033309"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["108(5)"],"pubmed_abstract":["Enterotoxigenic Bacteroides fragilis is the most frequent disease-causing anaerobe in the intestinal tract of humans and livestock and its specific virulence factor is fragilysin, also known as B. fragilis toxin. This is a 21-kDa zinc-dependent metallopeptidase existing in three closely related isoforms that hydrolyze E-cadherin and contribute to secretory diarrhea, and possibly to inflammatory bowel disease and colorectal cancer. Here we studied the function and zymogenic structure of fragilysin-3 and found that its activity is repressed by a ∼170-residue prodomain, which is the largest hitherto structurally characterized for a metallopeptidase. This prodomain plays a role in both the latency and folding stability of the catalytic domain and it has no significant sequence similarity to an"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog."],"pmcid":["PMC3033309"],"funding_grant_id":["FP7_223101","FP7_261460"],"pubmed_authors":["Arolas JL","Gomis-Ruth FX","Goulas T"],"additional_accession":[]},"is_claimable":false,"name":"Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog.","description":"Enterotoxigenic Bacteroides fragilis is the most frequent disease-causing anaerobe in the intestinal tract of humans and livestock and its specific virulence factor is fragilysin, also known as B. fragilis toxin. This is a 21-kDa zinc-dependent metallopeptidase existing in three closely related isoforms that hydrolyze E-cadherin and contribute to secretory diarrhea, and possibly to inflammatory bowel disease and colorectal cancer. Here we studied the function and zymogenic structure of fragilysin-3 and found that its activity is repressed by a ∼170-residue prodomain, which is the largest hitherto structurally characterized for a metallopeptidase. This prodomain plays a role in both the latency and folding stability of the catalytic domain and it has no significant sequence similarity to an","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Feb","modification":"2026-04-13T13:46:20.439Z","creation":"2019-03-27T00:38:40Z"},"accession":"S-EPMC3033309","cross_references":{"pubmed":["21233422"],"doi":["10.1073/pnas.1012173108"]}}