1sr4

Crystal Structure of the Haemophilus ducreyi cytolethal distending toxin

spinqualitylabelsall models 1sr4, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1sr4 is a 3 chain structure with sequence from "bacillus_ulceris_cancrosi"_kruse_1896 "bacillus ulceris cancrosi" kruse 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BR Gene: CDTA, HD0902 ("Bacillus ulceris cancrosi" Kruse 1896) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CDTA_HAEDU] CDTs are cytotoxins which induce host cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. CdtA, along with CdtC, probably forms a heterodimeric subunit required for the delivery of CdtB. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The tripartite cytolethal distending toxin (CDT) induces cell cycle arrest and apoptosis in eukaryotic cells. The subunits CdtA and CdtC associate with the nuclease CdtB to form a holotoxin that translocates CdtB into the host cell, where it acts as a genotoxin by creating DNA lesions. Here we show that the crystal structure of the holotoxin from Haemophilus ducreyi reveals that CDT consists of an enzyme of the DNase-I family, bound to two ricin-like lectin domains. CdtA, CdtB and CdtC form a ternary complex with three interdependent molecular interfaces, characterized by globular, as well as extensive non-globular, interactions. The lectin subunits form a deeply grooved, highly aromatic surface that we show to be critical for toxicity. The holotoxin possesses a steric block of the CdtB active site by means of a non-globular extension of the CdtC subunit, and we identify putative DNA binding residues in CdtB that are essential for toxin activity. Assembly and function of a bacterial genotoxin.,Nesic D, Hsu Y, Stebbins CE Nature. 2004 May 27;429(6990):429-33. PMID:15164065 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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