1OJG

Sensory domain of the membraneous two-component fumarate sensor DcuS of E. coli

Summary for 1OJG

• Entry DOI: 10.2210/pdb1ojg/pdb
• Descriptor: SENSOR PROTEIN DCUS (1 entity in total)
• Functional Keywords: transferase, fumarate, dcus, histidine kinase
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 15099.13

Authors

Pappalardo, L.,Janausch, I.G.,Vijayan, V.,Zientz, E.,Junker, J.,Peti, W.,Zweckstetter, M.,Unden, G.,Griesinger, C. (deposition date: 2003-07-10, release date: 2003-08-15, Last modification date: 2024-05-15)

Primary citation

Pappalardo, L.,Janausch, I.G.,Vijayan, V.,Zientz, E.,Junker, J.,Peti, W.,Zweckstetter, M.,Unden, G.,Griesinger, C.
The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.
J. Biol. Chem., 278:39185-39188, 2003

PubMed Abstract: 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.

PubMed: 12907689
DOI: 10.1074/jbc.C300344200

Experimental method

SOLUTION NMR