2F9Z

Complex between the chemotaxis deamidase CheD and the chemotaxis phosphatase CheC from Thermotoga maritima

Summary for 2F9Z

• Entry DOI: 10.2210/pdb2f9z/pdb
• Descriptor: chemotaxis protein CheC, PROTEIN (chemotaxis methylation protein) (3 entities in total)
• Functional Keywords: bacterial chemotaxis, signal transduction, receptor deamidase, aspartyl phosphatase, protein complex, reciprocal regulation, signaling protein
• Biological source: Thermotoga maritima; More
• Total number of polymer chains: 4
• Total formula weight: 78922.53

Authors

Chao, X.,Park, S.Y.,Bilwes, A.M.,Crane, B.R. (deposition date: 2005-12-06, release date: 2006-06-06, Last modification date: 2023-08-30)

Primary citation

Chao, X.,Muff, T.J.,Park, S.Y.,Zhang, S.,Pollard, A.M.,Ordal, G.W.,Bilwes, A.M.,Crane, B.R.
A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation.
Cell(Cambridge,Mass.), 124:561-571, 2006

PubMed Abstract: 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.

PubMed: 16469702
DOI: 10.1016/j.cell.2005.11.046

Experimental method

X-RAY DIFFRACTION (2.4 Å)