2f9z
Complex between the chemotaxis deamidase CheD and the chemotaxis phosphatase CheC from Thermotoga maritima
OverviewOverview
Signal transduction underlying bacterial chemotaxis involves excitatory phosphorylation and feedback control through deamidation and methylation of sensory receptors. The structure of a complex between the signal-terminating phosphatase, CheC, and the receptor-modifying deamidase, CheD, reveals how CheC mimics receptor substrates to inhibit CheD and how CheD stimulates CheC phosphatase activity. CheD resembles other cysteine deamidases from bacterial pathogens that inactivate host Rho-GTPases. CheD not only deamidates receptor glutamine residues contained within a conserved structural motif but also hydrolyzes glutamyl-methyl-esters at select regulatory positions. Substituting Gln into the receptor motif of CheC turns the inhibitor into a CheD substrate. Phospho-CheY, the intracellular signal and CheC target, stabilizes the CheC:CheD complex and reduces availability of CheD. A point mutation that dissociates CheC from CheD impairs chemotaxis in vivo. Thus, CheC incorporates an element of an upstream receptor to influence both its own effect on receptor output and that of its binding partner, CheD.
About this StructureAbout this Structure
2F9Z is a Protein complex structure of sequences from Thermotoga maritima msb8. Full crystallographic information is available from OCA.
ReferenceReference
A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation., Chao X, Muff TJ, Park SY, Zhang S, Pollard AM, Ordal GW, Bilwes AM, Crane BR, Cell. 2006 Feb 10;124(3):561-71. PMID:16469702 Page seeded by OCA on Sun May 4 03:38:47 2008