{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Estevan-Morio E"],"funding":["Spanish Ministry of Science and Innovation (MICINN)","Consejo Superior de Investigaciones Científicas","Government of Catalonia","Ministerio de Ciencia, Innovación y Universidades","JAE-Intro fellowship","Consolidated Research Group (SGR) project of the Generalitat de Catalunya"],"pagination":["1604"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11674741"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(12)"],"pubmed_abstract":["Cytophaga is a genus of Gram-negative bacteria occurring in soil and the gut microbiome. It is closely related to pathogenic <i>Flavobacterium</i> spp. that cause severe diseases in fish. Cytophaga strain L43-1 secretes cytophagalysin (CPL1), a 137 kDa peptidase with reported collagenolytic and gelatinolytic activity. We performed highly-confident structure prediction calculations for CPL1, which identified 11 segments and domains, including a signal peptide for secretion, a prosegment (PS) for latency, a metallopeptidase (MP)-like catalytic domain (CD), and eight immunoglobulin (Ig)-like domains (D3-D10). In addition, two short linkers were found at the D8-D9 and D9-D10 junctions, and the structure would be crosslinked by four disulfide bonds. The CPL1 CD was found closest to ulilysin fro"],"journal":["Biomolecules"],"pubmed_title":["Dissecting Cytophagalysin: Structural and Biochemical Studies of a Bacterial Pappalysin-Family Metallopeptidase."],"pmcid":["PMC11674741"],"funding_grant_id":["RYC2020-029773-I","PRE2020-096731","2021SGR00423","JAEINT_22_02654","PID2021-128682OA-I00"],"pubmed_authors":["Bushi E","Estevan-Morio E","Ramirez-Larrota JS","Eckhard U"],"additional_accession":[]},"is_claimable":false,"name":"Dissecting Cytophagalysin: Structural and Biochemical Studies of a Bacterial Pappalysin-Family Metallopeptidase.","description":"Cytophaga is a genus of Gram-negative bacteria occurring in soil and the gut microbiome. It is closely related to pathogenic <i>Flavobacterium</i> spp. that cause severe diseases in fish. Cytophaga strain L43-1 secretes cytophagalysin (CPL1), a 137 kDa peptidase with reported collagenolytic and gelatinolytic activity. We performed highly-confident structure prediction calculations for CPL1, which identified 11 segments and domains, including a signal peptide for secretion, a prosegment (PS) for latency, a metallopeptidase (MP)-like catalytic domain (CD), and eight immunoglobulin (Ig)-like domains (D3-D10). In addition, two short linkers were found at the D8-D9 and D9-D10 junctions, and the structure would be crosslinked by four disulfide bonds. The CPL1 CD was found closest to ulilysin fro","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-05-26T20:10:17.763Z","creation":"2026-05-25T03:07:09.427Z"},"accession":"S-EPMC11674741","cross_references":{"pubmed":["39766312"],"doi":["10.3390/biom14121604"]}}