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• W2108622832 endingPage "1096" @default.
• W2108622832 startingPage "1093" @default.
• W2108622832 abstract "The 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." @default.
• W2108622832 created "2016-06-24" @default.
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• W2108622832 date "2005-08-12" @default.
• W2108622832 modified "2023-09-30" @default.
• W2108622832 title "Structural Basis for the Activation of Cholera Toxin by Human ARF6-GTP" @default.
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• W2108622832 doi "https://doi.org/10.1126/science.1113398" @default.
• W2108622832 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16099990" @default.
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