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{
"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
}
}
