Science · 2017 · 61 citations · 31 references
Life SciencesBiochemistryMolecular BiologyCell SignalingCytoskeletonSignal TransductionBacterial ToxinsSmall Gtpase SignalingToxin-mediated PathogenesisBacterial Toxin BiologyLipid AcylationPathogenesis Of Bacterial ToxinsProtein ToxinsRho Family Gtpase SignalingRho Family GtpasesSmall Rho Gtpase SignalingToxin Function
Bacterial toxin fatty-acylates lysine residues A toxin produced by the bacterium that causes cholera has a catalytic activity that contributes to its effects on the cytoskeleton of host cells. Zhou et al. determined the protein structure of the Rho guanosine triphosphatase (GTPase)–inactivation domain of the toxin from Vibrio cholerae and found it to be similar to that of a human fatty acyltransferase. Indeed, the toxin peptide could catalyze fatty acylation of lysine residues of Rho-family GTPases, which regulate the actin cytoskeleton. Such covalent modification of lysine residues in mammalian proteins had been noted before, but the enzymes responsible were not known. Science , this issue p. 528
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Dali server: conservation mapping in 3D
Liisa Holm · Nucleic Acids Research · 2010 · 3.7K citations · Full text