title: Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins.
abstract: Over the past few decades, our understanding of the bacterial protein toxins that modulate G proteins has advanced tremendously through extensive biochemical and structural analyses. This article provides an updated survey of the various toxins that target G proteins, ending with a focus on recent mechanistic insights in our understanding of the deamidating toxin family. The dermonecrotic toxin from Pasteurella multocida (PMT) was recently added to the list of toxins that disrupt G-protein signal transduction through selective deamidation of their targets. The C3 deamidase domain of PMT has no sequence similarity to the deamidase domains of the dermonecrotic toxins from Escherichia coli (cytotoxic necrotizing factor [CNF]1-3), Yersinia (CNFY) and Bordetella (dermonecrotic toxin). The structure of PMT-C3 belongs to a family of transglutaminase-like proteins, with active site Cys-His-Asp catalytic triads distinct from E. coli CNF1.
authors: Department of Microbiology and Institute for Genomic Biology, University of Illinois at Urbana-Champaign, 601 S. Goodwin Ave, B128 CLSL, Urbana, IL 61801, USA. bawilson@life.illinois.edu
authors: Brenda A
authors: BA
authors: Wilson
authors: Mengfei
authors: M
authors: Ho
mesh_terms: D001427:Bacterial Toxins / Q000378:metabolism*; D001884:Bordetella / Q000472:pathogenicity; D003603:Cytotoxins / Q000378:metabolism*; D003641:Deamination; D004926:Escherichia coli / Q000472:pathogenicity; D019204:GTP-Binding Proteins / Q000037:antagonists & inhibitors*; D008954:Models, Biological; D016979:Pasteurella multocida / Q000472:pathogenicity; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction / Q000187:drug effects*; D015007:Yersinia / Q000472:pathogenicity
chemical_list: D001427:Bacterial Toxins; D003603:Cytotoxins; D019204:GTP-Binding Proteins