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{
    "metadata": {
        "accession": "IPR022406",
        "entry_id": null,
        "type": "domain",
        "go_terms": null,
        "source_database": "interpro",
        "member_databases": {
            "pfam": {
                "PF02763": "Diphtheria toxin, C domain"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR022406",
            "name": "Diphtheria toxin, catalytic domain",
            "type": "Domain",
            "children": []
        },
        "name": {
            "name": "Diphtheria toxin, catalytic domain",
            "short": "Diphtheria_toxin_catalytic_dom"
        },
        "description": [
            {
                "text": "<p>This entry represents the N-terminal catalytic domain (also known as the C domain). This domain has an unusual β+α fold [[cite:PUB00037609]]. The C domain blocks protein synthesis by transfer of ADP-ribose from NAD to a diphthamide residue of EF-2 [[cite:PUB00005016], [cite:PUB00000429]].</p>",
                "llm": false,
                "checked": false,
                "updated": false
            },
            {
                "text": "<p>Diphtheria toxin ([ec:2.4.2.36]) is a 58kDa protein secreted by lysogenic strains of Corynebacterium diphtheriae. The toxin causes the disease diphtheria in humans by gaining entry into the cell cytoplasm and inhibiting protein synthesis [[cite:PUB00000429]]. The mechanism of inhibition involves transfer of the ADP-ribose group of NAD to elongation factor-2 (EF-2), rendering EF-2 inactive. The catalysed reaction is as follows:</p>\n\n<p>\n<reaction>\nNAD<sup>+</sup> + peptide diphthamide = nicotinamide + peptide N-(ADP-D-ribosyl)diphthamide\n</reaction>\n</p>\n\n<p>The crystal structure of the diphtheria toxin homodimer has been determined to 2.5A resolution [[cite:PUB00004122]]. The structure reveals a Y-shaped molecule of 3 domains, a catalytic domain (fragment A), whose fold is of the α+β type; a transmembrane (TM) domain, which consists of 9 α-helices, 2 pairs of which may participate in pH-triggered membrane insertion and translocation; and a receptor-binding domain, which forms a flattened β-barrel with a jelly-roll-like topology [[cite:PUB00004122]]. The TM- and receptor binding-domains together constitute fragment B.</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00037609": {
                "PMID": 9012663,
                "ISBN": null,
                "volume": "36",
                "issue": "3",
                "year": 1997,
                "title": "Crystal structure of nucleotide-free diphtheria toxin.",
                "URL": null,
                "raw_pages": "481-8",
                "medline_journal": "Biochemistry",
                "ISO_journal": "Biochemistry",
                "authors": [
                    "Bell CE",
                    "Eisenberg D."
                ],
                "DOI_URL": "http://dx.doi.org/10.1021/bi962214s"
            },
            "PUB00005016": {
                "PMID": 7833808,
                "ISBN": null,
                "volume": "3",
                "issue": "9",
                "year": 1994,
                "title": "Refined structure of monomeric diphtheria toxin at 2.3 A resolution.",
                "URL": null,
                "raw_pages": "1464-75",
                "medline_journal": "Protein Sci",
                "ISO_journal": "Protein Sci.",
                "authors": [
                    "Bennett MJ",
                    "Eisenberg D."
                ],
                "DOI_URL": "http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7833808&action=stream&blobtype=pdf"
            },
            "PUB00000429": {
                "PMID": 8573568,
                "ISBN": null,
                "volume": "35",
                "issue": "4",
                "year": 1996,
                "title": "Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide.",
                "URL": null,
                "raw_pages": "1137-49",
                "medline_journal": "Biochemistry",
                "ISO_journal": "Biochemistry",
                "authors": [
                    "Bell CE",
                    "Eisenberg D."
                ],
                "DOI_URL": "http://dx.doi.org/10.1021/bi9520848"
            },
            "PUB00004122": {
                "PMID": 1589020,
                "ISBN": null,
                "volume": "357",
                "issue": "6375",
                "year": 1992,
                "title": "The crystal structure of diphtheria toxin.",
                "URL": null,
                "raw_pages": "216-22",
                "medline_journal": "Nature",
                "ISO_journal": "Nature",
                "authors": [
                    "Choe S",
                    "Bennett MJ",
                    "Fujii G",
                    "Curmi PM",
                    "Kantardjieff KA",
                    "Collier RJ",
                    "Eisenberg D."
                ],
                "DOI_URL": "http://dx.doi.org/10.1038/357216a0"
            }
        },
        "set_info": null,
        "overlaps_with": null,
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 4,
            "interactions": 0,
            "matches": 42,
            "pathways": 1,
            "proteins": 42,
            "proteomes": 15,
            "sets": 0,
            "structural_models": {
                "alphafold": 30,
                "bfvd": 0
            },
            "structures": 21,
            "taxa": 57
        },
        "entry_annotations": {
            "alignment:seed": 1,
            "alignment:full": 6
        },
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": null
    }
}