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2f9z

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Current revision

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

Structural highlights

2f9z is a 4 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHEC_THEMA Involved in restoring normal CheY-P levels by dephosphorylating CheY-P. Inhibits CheD by incorporating in its fold a structural motif that mimics a CheD substrate recognition site to bait and inactivate it.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chao X, Muff TJ, Park SY, Zhang S, Pollard AM, Ordal GW, Bilwes AM, Crane BR. A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation. Cell. 2006 Feb 10;124(3):561-71. PMID:16469702 doi:http://dx.doi.org/10.1016/j.cell.2005.11.046

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2f9z"

@@ Line 1: / Line 1: @@
 ==Complex between the chemotaxis deamidase CheD and the chemotaxis phosphatase CheC from Thermotoga maritima==
-<StructureSection load='2f9z' size='340' side='right' caption='[[2f9z]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='2f9z' size='340' side='right'caption='[[2f9z]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2f9z]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F9Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2f9z]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F9Z FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM0904 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA]), TM0903 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9z OCA], [http://pdbe.org/2f9z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f9z RCSB], [http://www.ebi.ac.uk/pdbsum/2f9z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f9z ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9z OCA], [https://pdbe.org/2f9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f9z RCSB], [https://www.ebi.ac.uk/pdbsum/2f9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f9z ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CHEC_THEMA CHEC_THEMA]] Involved in restoring normal CheY-P levels by dephosphorylating CheY-P. Inhibits CheD by incorporating in its fold a structural motif that mimics a CheD substrate recognition site to bait and inactivate it. [[http://www.uniprot.org/uniprot/CHED_THEMA CHED_THEMA]] Deamidates glutamine residues on chemoreceptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase. In addition, demethylates methylated glutamate residues on chemoreceptors Mcp2 and Mcp4. Enhances the activity of CheC.
+[https://www.uniprot.org/uniprot/CHEC_THEMA CHEC_THEMA] Involved in restoring normal CheY-P levels by dephosphorylating CheY-P. Inhibits CheD by incorporating in its fold a structural motif that mimics a CheD substrate recognition site to bait and inactivate it.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 </div>
 <div class="pdbe-citations 2f9z" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Thema]]
+[[Category: Large Structures]]
-[[Category: Bilwes, A M]]
+[[Category: Thermotoga maritima MSB8]]
-[[Category: Chao, X]]
+[[Category: Bilwes AM]]
-[[Category: Crane, B R]]
+[[Category: Chao X]]
-[[Category: Park, S Y]]
+[[Category: Crane BR]]
-[[Category: Aspartyl phosphatase]]
+[[Category: Park SY]]
-[[Category: Bacterial chemotaxis]]
-[[Category: Protein complex]]
-[[Category: Receptor deamidase]]
-[[Category: Reciprocal regulation]]
-[[Category: Signal transduction]]
-[[Category: Signaling protein]]

2f9z

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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