2c8h | pdb_00002c8h

Structure of the PN loop Q182A mutant C3bot1 Exoenzyme (NAD-bound state, crystal form I)

spinqualitylabelsall models 2c8h, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c8h is a 4 chain structure with sequence from "bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAD, SO4 Related: 1g24, 1gze, 1gzf, 1uzi, 2a78, 2a9k, 2bov, 2c89, 2c8a, 2c8b, 2c8c, 2c8d, 2c8e, 2c8f, 2c8g Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ARC3_CBDP] ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue. 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 We have solved the crystal structures of Clostridium botulinum C3 exoenzyme free and complexed to NAD in the same crystal form, at 2.7 and 1.95 A, respectively. The asymmetric unit contains four molecules, which, in the free form, share the same conformation. Upon NAD binding, C3 underwent various conformational changes, whose amplitudes were differentially limited in the four molecules of the crystal unit. A major rearrangement concerns the loop that contains the functionally important ARTT motif (ADP-ribosyltransferase toxin turn-turn). The ARTT loop undergoes an ample swinging motion to adopt a conformation that covers the nicotinamide moiety of NAD. In particular, Gln-212, which belongs to the ARTT motif, flips over from a solvent-exposed environment to a buried conformation in the NAD binding pocket. Mutational experiments showed that Gln-212 is neither involved in NAD binding nor in the NAD-glycohydrolase activity of C3, whereas it plays a critical role in the ADP-ribosyl transfer to the substrate Rho. We observed additional NAD-induced movements, including a crab-claw motion of a subdomain that closes the NAD binding pocket. The data emphasized a remarkable NAD-induced plasticity of the C3 binding pocket and suggest that the NAD-induced ARTT loop conformation may be favored by the C3-NAD complex to bind to the substrate Rho. Our structural observations, together with a number of mutational experiments suggest that the mechanisms of Rho ADP-ribosylation by C3-NAD may be more complex than initially anticipated. NAD binding induces conformational changes in Rho ADP-ribosylating clostridium botulinum C3 exoenzyme.,Menetrey J, Flatau G, Stura EA, Charbonnier JB, Gas F, Teulon JM, Le Du MH, Boquet P, Menez A J Biol Chem. 2002 Aug 23;277(34):30950-7. Epub 2002 May 23. PMID:12029083 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Exoenzyme 3D structures

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