{"metadata":{"accession":"cd20229","entry_id":null,"type":"domain","go_terms":null,"source_database":"cdd","member_databases":null,"integrated":null,"hierarchy":null,"name":{"name":"pore-forming module (PFM) of uncharacterized proteins having tachylectin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins","short":"PFM_tachylectin-like"},"description":[{"text":"<p>Many proteins belonging to this group have tachylectin domain(s), N-terminal to this PFM; some also have an immunoglobulin (Ig) domain. Tachylectins are lectins which bind N-acetylglucosamine and N-acetylgalactosamine. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). [[cite:PUB00106999], [cite:PUB00107000], [cite:PUB00107001], [cite:PUB00107002], [cite:PUB00107003], [cite:PUB00107004], [cite:PUB00107005]]</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00107001":{"PMID":27176125,"ISBN":null,"volume":"7","issue":null,"year":2016,"title":"Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly.","URL":null,"raw_pages":"11598","medline_journal":"Nat Commun","ISO_journal":"Nat Commun","authors":["Podobnik M","Savory P","Rojko N","Kisovec M","Wood N","Hambley R","Pugh J","Wallace EJ","McNeill L","Bruce M","Liko I","Allison TM","Mehmood S","Yilmaz N","Kobayashi T","Gilbert RJ","Robinson CV","Jayasinghe L","Anderluh G."],"DOI_URL":null},"PUB00107003":{"PMID":21687664,"ISBN":null,"volume":"6","issue":"6","year":2011,"title":"Extending the aerolysin family: from bacteria to vertebrates.","URL":null,"raw_pages":"e20349","medline_journal":"PLoS One","ISO_journal":"PLoS One","authors":["Szczesny P","Iacovache I","Muszewska A","Ginalski K","van der Goot FG","Grynberg M."],"DOI_URL":null},"PUB00106999":{"PMID":20482872,"ISBN":null,"volume":"10","issue":null,"year":2010,"title":"High amino acid diversity and positive selection at a putative coral immunity gene (tachylectin-2).","URL":null,"raw_pages":"150","medline_journal":"BMC Evol Biol","ISO_journal":"BMC Evol Biol","authors":["Hayes ML","Eytan RI","Hellberg ME."],"DOI_URL":null},"PUB00107002":{"PMID":28630149,"ISBN":null,"volume":"372","issue":"1726","year":2017,"title":"Molecular mechanism of pore formation by aerolysin-like proteins. ","URL":null,"raw_pages":"20160209","medline_journal":"Philos Trans R Soc Lond B Biol Sci","ISO_journal":"Philos Trans R Soc Lond B Biol Sci","authors":["Podobnik M","Kisovec M","Anderluh G."],"DOI_URL":null},"PUB00107004":{"PMID":20687481,"ISBN":null,"volume":"677","issue":null,"year":2010,"title":"Laetiporus sulphureus lectin and aerolysin protein family.","URL":null,"raw_pages":"67-80","medline_journal":"Adv Exp Med Biol","ISO_journal":"Adv Exp Med Biol","authors":["Mancheno JM","Tateno H","Sher D","Goldstein IJ."],"DOI_URL":null},"PUB00107000":{"PMID":29066778,"ISBN":null,"volume":"7","issue":"1","year":2017,"title":"Structural, physicochemical and dynamic features conserved within the aerolysin pore-forming toxin family.","URL":null,"raw_pages":"13932","medline_journal":"Sci Rep","ISO_journal":"Sci Rep","authors":["Cirauqui N","Abriata LA","van der Goot FG","Dal Peraro M."],"DOI_URL":null},"PUB00107005":{"PMID":14715670,"ISBN":null,"volume":"279","issue":"14","year":2004,"title":"The identification and structure of the membrane-spanning domain of the Clostridium septicum alpha toxin.","URL":null,"raw_pages":"14315-22","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Melton JA","Parker MW","Rossjohn J","Buckley JT","Tweten RK."],"DOI_URL":null}},"set_info":{"accession":"cl40431","name":"PFM_aerolysin_family"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":69,"pathways":0,"proteins":61,"proteomes":6,"sets":1,"structural_models":{"alphafold":50,"bfvd":0},"structures":0,"taxa":45},"entry_annotations":{},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}