6533b7d2fe1ef96bd125eb98
RESEARCH PRODUCT
The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli
Gottfried UndenVinesh VijayanLucia PappalardoWolfgang PetiIngo G. JanauschJochen JunkerMarkus ZweckstetterEva ZientzChristian Griesingersubject
Models MolecularProtein FoldingMagnetic Resonance SpectroscopyProtein ConformationStereochemistryMolecular Sequence DataReceptors Cell SurfaceBiologyArginineBiochemistryProtein Structure SecondaryBacterial ProteinsFumaratesEscherichia coliTransferaseHistidineAmino Acid SequenceProtein kinase AMolecular BiologyHistidineBinding SitesEscherichia coli ProteinsC-terminusCell MembraneHistidine kinaseCell BiologyNuclear magnetic resonance spectroscopyPeriplasmic spaceChemoreceptor CellsTransmembrane proteinProtein Structure TertiaryCrystallographyMutationPeriplasmProtein KinasesSignal Transductiondescription
The structure of the water-soluble, periplasmic domain of the fumarate sensor DcuS (DcuS-pd) has been determined by NMR spectroscopy in solution. DcuS is a prototype for a sensory histidine kinase with transmembrane signal transfer. DcuS belongs to the CitA family of sensors that are specific for sensing di- and tricarboxylates. The periplasmic domain is folded autonomously and shows helices at the N and the C terminus, suggesting direct linking or connection to helices in the two transmembrane regions. The structure constitutes a novel fold. The nearest structural neighbor is the Per-Arnt-Sim domain of the photoactive yellow protein that binds small molecules covalently. Residues Arg107, His110, and Arg147 are essential for fumarate sensing and are found clustered together. The structure constitutes the first periplasmic domain of a two component sensory system and is distinctly different from the aspartate sensory domain of the Tar chemotaxis sensor.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2003-10-03 |