3ny6 | pdb_00003ny6

Catalytic fragment of cholix toxin from vibrio cholerae in complex with inhibitor V30

spinqualitylabelsall models 3ny6, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ny6 is a 1 chain structure with sequence from "bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, PO4, V30 Related: 2q6m, 3ess, 3ki0, 3ki1, 3ki2, 3ki3, 3ki4, 3ki5, 3ki6, 3ki7 Gene: chxa, toxA ("Bacillo virgola del Koch" Trevisan 1884) Activity: NAD(+)--diphthamide ADP-ribosyltransferase, with EC number 2.4.2.36 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CHXA_VIBCL] An NAD-dependent ADP-ribosyltransferase (ADPRT), it catalyzes the transfer of the ADP-ribosyl moiety of oxidized NAD onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. It probably uses the eukaryotic prolow-density lipoprotein receptor-related protein 1 (LRP1) to enter mouse cells, although there seems to be at least one other receptor as well. Is active against mouse fibroblasts, Chinese hamster ovary eEF-2, brine shrimp (Artemia spp. nauplii) and upon expression in S.cerevisiae. Publication Abstract from PubMed The mono-ADP-ribosyltransferase toxins are bacterial virulence factors that contribute to many disease states in plants, animals and humans. These toxins function as enzymes that target various host proteins and covalently attach an ADP-ribose moiety that alters target protein function. We tested compounds from a virtual screen of commercially available compounds combined with a directed PARP inhibitor library and found several compounds that bind tightly and inhibit toxins from Pseudomonas aeruginosa and Vibrio cholerae. The most efficacious compounds completely protected human lung epithelial cells against the cytotoxicity of these bacterial virulence factors. Moreover, we determined high-resolution crystal structures of the best inhibitors in complex with cholix toxin to reveal important criteria for inhibitor binding and mechanism of action. These results provide new insight in antivirulence compound development for treating many bacterial diseases. Newly Discovered and Characterized Antivirulence Compounds inhibit Bacterial Mono-ADP-ribosyltransferase Toxins.,Turgeon Z, Jorgensen R, Visschedyk D, Edwards PR, Legree S, McGregor C, Fieldhouse RJ, Mangroo D, Schapira M, Merrill AR Antimicrob Agents Chemother. 2010 Dec 6. PMID:21135177 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Exotoxin 3D structures

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