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[[Image:2tmy.jpg|left|200px]]
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{{STRUCTURE_2tmy|  PDB=2tmy  |  SCENE=  }}
'''CHEY FROM THERMOTOGA MARITIMA (APO-II)'''


==CHEY FROM THERMOTOGA MARITIMA (APO-II)==
<StructureSection load='2tmy' size='340' side='right'caption='[[2tmy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2tmy]] 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=2TMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TMY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=2tmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tmy OCA], [https://pdbe.org/2tmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tmy RCSB], [https://www.ebi.ac.uk/pdbsum/2tmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tmy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CHEY_THEMA CHEY_THEMA] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheY seems to regulate the clockwise (CW) rotation (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tm/2tmy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2tmy ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of CheY protein from Thermotoga maritima has been determined in four crystal forms with and without Mg++ bound, at up to 1.9 A resolution. Structural comparisons with CheY from Escherichia coli shows substantial similarity in their folds, with some concerted changes propagating away from the active site that suggest how phosphorylated CheY, a signal transduction protein in bacterial chemotaxis, is recognized by its targets. A highly conserved segment of the protein (the "y-turn loop," residues 55-61), previously suggested to be a rigid recognition determinant, is for the first time seen in two alternative conformations in the different crystal structures. Although CheY from Thermotoga has much higher thermal stability than its mesophilic counterparts, comparison of structural features previously proposed to enhance thermostability such as hydrogen bonds, ion pairs, compactness, and hydrophobic surface burial would not suggest it to be so.


==Overview==
Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability.,Usher KC, de la Cruz AF, Dahlquist FW, Swanson RV, Simon MI, Remington SJ Protein Sci. 1998 Feb;7(2):403-12. PMID:9521117<ref>PMID:9521117</ref>
The crystal structure of CheY protein from Thermotoga maritima has been determined in four crystal forms with and without Mg++ bound, at up to 1.9 A resolution. Structural comparisons with CheY from Escherichia coli shows substantial similarity in their folds, with some concerted changes propagating away from the active site that suggest how phosphorylated CheY, a signal transduction protein in bacterial chemotaxis, is recognized by its targets. A highly conserved segment of the protein (the "y-turn loop," residues 55-61), previously suggested to be a rigid recognition determinant, is for the first time seen in two alternative conformations in the different crystal structures. Although CheY from Thermotoga has much higher thermal stability than its mesophilic counterparts, comparison of structural features previously proposed to enhance thermostability such as hydrogen bonds, ion pairs, compactness, and hydrophobic surface burial would not suggest it to be so.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2TMY 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=2TMY OCA].
</div>
<div class="pdbe-citations 2tmy" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability., Usher KC, de la Cruz AF, Dahlquist FW, Swanson RV, Simon MI, Remington SJ, Protein Sci. 1998 Feb;7(2):403-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9521117 9521117]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Cruz, A De La.]]
[[Category: Dahlquist FW]]
[[Category: Dahlquist, F W.]]
[[Category: De La Cruz A]]
[[Category: Remington, S J.]]
[[Category: Remington SJ]]
[[Category: Usher, K C.]]
[[Category: Usher KC]]
[[Category: Chemotaxis]]
[[Category: Phosphoryl transfer]]
[[Category: Signal transduction]]
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Retrieved from "https://proteopedia.org/2tmy"