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| | <StructureSection load='2f9z' size='340' side='right'caption='[[2f9z]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2f9z' size='340' side='right'caption='[[2f9z]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2f9z]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/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 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA]), TM0903 ([https://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]] 2.4Å</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> | | <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> | | </table> |
| | == Function == | | == Function == |
| - | [[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. [[https://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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thema]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Bilwes, A M]] | + | [[Category: Bilwes AM]] |
| - | [[Category: Chao, X]] | + | [[Category: Chao X]] |
| - | [[Category: Crane, B R]] | + | [[Category: Crane BR]] |
| - | [[Category: Park, S Y]] | + | [[Category: Park SY]] |
| - | [[Category: Aspartyl phosphatase]]
| + | |
| - | [[Category: Bacterial chemotaxis]]
| + | |
| - | [[Category: Protein complex]]
| + | |
| - | [[Category: Receptor deamidase]]
| + | |
| - | [[Category: Reciprocal regulation]]
| + | |
| - | [[Category: Signal transduction]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
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.
See Also
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
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