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Structural basis for the activation of cholera toxin by human ARF6-GTP O'Neal CJ; Jobling MG; Holmes RK; Hol WGScience 2005[Aug]; 309 (5737): 1093-6The Vibrio cholerae bacterium causes devastating diarrhea when it infects the human intestine. The key event is adenosine diphosphate (ADP)-ribosylation of the human signaling protein GSalpha, catalyzed by the cholera toxin A1 subunit (CTA1). This reaction is allosterically activated by human ADP-ribosylation factors (ARFs), a family of essential and ubiquitous G proteins. Crystal structures of a CTA1:ARF6-GTP (guanosine triphosphate) complex reveal that binding of the human activator elicits dramatic changes in CTA1 loop regions that allow nicotinamide adenine dinucleotide (NAD+) to bind to the active site. The extensive toxin:ARF-GTP interface surface mimics ARF-GTP recognition of normal cellular protein partners, which suggests that the toxin has evolved to exploit promiscuous binding properties of ARFs.|ADP-Ribosylation Factor 6[MESH]|ADP-Ribosylation Factors/*chemistry/genetics/*metabolism[MESH]|Amino Acid Sequence[MESH]|Binding Sites[MESH]|Cholera Toxin/*chemistry/genetics/*metabolism[MESH]|Crystallography, X-Ray[MESH]|Dimerization[MESH]|Evolution, Molecular[MESH]|Guanosine Diphosphate/metabolism[MESH]|Guanosine Triphosphate/*chemistry/*metabolism[MESH]|Humans[MESH]|Hydrophobic and Hydrophilic Interactions[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|NAD/metabolism[MESH]|Protein Binding[MESH]|Protein Conformation[MESH]|Protein Structure, Secondary[MESH] |
