1xkr

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[[Image:1xkr.gif|left|200px]]
 
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==X-ray Structure of Thermotoga maritima CheC==
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The line below this paragraph, containing "STRUCTURE_1xkr", creates the "Structure Box" on the page.
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<StructureSection load='1xkr' size='340' side='right'caption='[[1xkr]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1xkr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XKR FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xkr OCA], [https://pdbe.org/1xkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xkr RCSB], [https://www.ebi.ac.uk/pdbsum/1xkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xkr ProSAT]</span></td></tr>
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{{STRUCTURE_1xkr| PDB=1xkr | SCENE= }}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xk/1xkr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xkr ConSurf].
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<div style="clear:both"></div>
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'''X-ray Structure of Thermotoga maritima CheC'''
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==See Also==
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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In bacterial chemotaxis, phosphorylated CheY levels control the sense of flagella rotation and thereby determine swimming behavior. In E. coli, CheY dephosphorylation by CheZ extinguishes the switching signal. But, instead of CheZ, many chemotactic bacteria contain CheC, CheD, and/or CheX. The crystal structures of T. maritima CheC and CheX reveal a common fold unlike that of any other known protein. Unlike CheC, CheX dimerizes via a continuous beta sheet between subunits. T. maritima CheC, as well as CheX, dephosphorylate CheY, although CheC requires binding of CheD to achieve the activity of CheX. Structural analyses identified one conserved active site in CheX and two in CheC; mutations therein reduce CheY-phosphatase activity, but only mutants of two invariant asparagine residues are completely inactive even in the presence of CheD. Our structures indicate that the flagellar switch components FliY and FliM resemble CheC more closely than CheX, but attribute phosphatase activity only to FliY.
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[[Category: Large Structures]]
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==About this Structure==
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1XKR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKR OCA].
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==Reference==
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Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX., Park SY, Chao X, Gonzalez-Bonet G, Beel BD, Bilwes AM, Crane BR, Mol Cell. 2004 Nov 19;16(4):563-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15546616 15546616]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Beel, B D.]]
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[[Category: Beel BD]]
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[[Category: Bilwes, A M.]]
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[[Category: Bilwes AM]]
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[[Category: Chao, X.]]
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[[Category: Chao X]]
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[[Category: Crane, B R.]]
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[[Category: Crane BR]]
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[[Category: Gonzalez-Bonet, G.]]
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[[Category: Gonzalez-Bonet G]]
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[[Category: Park, S Y.]]
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[[Category: Park SY]]
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[[Category: Chemotaxis]]
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[[Category: Protein phosphatase]]
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[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:09:28 2008''
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Current revision

X-ray Structure of Thermotoga maritima CheC

PDB ID 1xkr

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