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 2.4&Aring;" /> '''Complex between the c...)
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[[Image:2f9z.gif|left|200px]]<br /><applet load="2f9z" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2f9z.gif|left|200px]]<br /><applet load="2f9z" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2f9z, resolution 2.4&Aring;" />
caption="2f9z, resolution 2.4&Aring;" />
'''Complex between the chemotaxis deamidase CheD and the chemotaxis phosphatase CheC from Thermotoga maritima'''<br />
'''Complex between the chemotaxis deamidase CheD and the chemotaxis phosphatase CheC from Thermotoga maritima'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2F9Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F9Z OCA].
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2F9Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9Z OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermotoga maritima msb8]]
[[Category: Thermotoga maritima msb8]]
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[[Category: Bilwes, A.M.]]
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[[Category: Bilwes, A M.]]
[[Category: Chao, X.]]
[[Category: Chao, X.]]
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[[Category: Crane, B.R.]]
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[[Category: Crane, B R.]]
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[[Category: Park, S.Y]]
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[[Category: Park, S Y]]
[[Category: aspartyl phosphatase]]
[[Category: aspartyl phosphatase]]
[[Category: bacterial chemotaxis]]
[[Category: bacterial chemotaxis]]
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[[Category: signal transduction]]
[[Category: signal transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:26:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:17 2008''

Revision as of 15:19, 21 February 2008


2f9z, resolution 2.4Å

Drag the structure with the mouse to rotate

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

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