1xkr
From Proteopedia
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<StructureSection load='1xkr' size='340' side='right'caption='[[1xkr]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='1xkr' size='340' side='right'caption='[[1xkr]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1xkr]] is a 1 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</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=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> | ||
</table> | </table> | ||
| + | == 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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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:15546616<ref>PMID:15546616</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1xkr" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 43589]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Beel | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Bilwes | + | [[Category: Beel BD]] |
| - | [[Category: Chao | + | [[Category: Bilwes AM]] |
| - | [[Category: Crane | + | [[Category: Chao X]] |
| - | [[Category: Gonzalez-Bonet | + | [[Category: Crane BR]] |
| - | [[Category: Park | + | [[Category: Gonzalez-Bonet G]] |
| - | + | [[Category: Park SY]] | |
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Current revision
X-ray Structure of Thermotoga maritima CheC
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