title: Cyclic di-GMP allosterically inhibits the CRP-like protein (Clp) of Xanthomonas axonopodis pv. citri.
abstract: The protein Clp from Xanthomonas axonopodis pv. citri regulates pathogenesis and is a member of the CRP (cyclic AMP receptor protein) superfamily. We show that unlike the DNA-binding activity of other members of this family, the DNA-binding activity of Clp is allosterically inhibited by its effector and that cyclic di-GMP serves as that effector at physiological concentrations.
authors.affiliation: Department of Bacteriology, 1550 Linden Drive, University of Wisconsin-Madison, Madison, WI 53706, USA.
authors.forename: Jason L
authors.initials: JL
authors.lastname: Leduc
authors.forename: Gary P
authors.initials: GP
authors.lastname: Roberts
mesh_terms: D000494:Allosteric Regulation / Q000235:genetics / Q000502:physiology*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D006152:Cyclic GMP / Q000031:analogs & derivatives* / Q000378:metabolism / Q000502:physiology; D004247:DNA / Q000378:metabolism; D005454:Fluorescence Polarization; D011485:Protein Binding; D053532:Xanthomonas axonopodis / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; C062025:bis(3',5')-cyclic diguanylic acid; D004247:DNA; D006152:Cyclic GMP