2f9z
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(New page: 200px<br /><applet load="2f9z" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f9z, resolution 2.4Å" /> '''Complex between the c...)
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Revision as of 08:19, 21 November 2007
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Complex between the chemotaxis deamidase CheD and the chemotaxis phosphatase CheC from Thermotoga maritima
Overview
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 Structure
2F9Z is a Protein complex structure of sequences from Thermotoga maritima msb8. Full crystallographic information is available from OCA.
Reference
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 Wed Nov 21 10:26:43 2007
