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New page: left|200px<br /><applet load="1chn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1chn, resolution 1.76Å" /> '''MAGNESIUM BINDING TO...
 
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[[Image:1chn.jpg|left|200px]]<br /><applet load="1chn" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1chn, resolution 1.76&Aring;" />
'''MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL CHANGES INVOLVING ITS FUNCTIONAL SURFACE'''<br />


==Overview==
==MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL CHANGES INVOLVING ITS FUNCTIONAL SURFACE==
The three-dimensional crystal structure of the bacterial chemotaxis, protein CheY with the essential Mg2+ cation bound to the active site, reveals large conformational changes caused by the metal binding., Displacements of up to 10 A are observed in several residues at the N, terminus of alpha-helix 4 and in the preceding loop. One turn of this, helix unwinds, and an Asn residue that was located inside the helix, becomes the new N-cap. This supports the important role that N or C-cap, residues play in alpha-helix stability. In addition the preceding, beta-strand becomes elongated and a new beta-turn appears. The final, effect is a significant modification of the surface relief of the protein, in a region previously indicated, by genetic analysis, to be essential for, CheY function. It is suggested that binding of a divalent cation to CheY, could play a significant part in CheY activation and consequently in, signal transduction in prokaryotes.
<StructureSection load='1chn' size='340' side='right'caption='[[1chn]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1chn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CHN FirstGlance]. <br>
1CHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CHN OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1chn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chn OCA], [https://pdbe.org/1chn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1chn RCSB], [https://www.ebi.ac.uk/pdbsum/1chn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1chn ProSAT]</span></td></tr>
Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface., Bellsolell L, Prieto J, Serrano L, Coll M, J Mol Biol. 1994 May 13;238(4):489-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8176739 8176739]
</table>
== Function ==
[https://www.uniprot.org/uniprot/CHEY_ECOLI CHEY_ECOLI] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator.<ref>PMID:20346719</ref>
== 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/ch/1chn_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=1chn ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bellsolell, L.]]
[[Category: Bellsolell L]]
[[Category: Coll, M.]]
[[Category: Coll M]]
[[Category: MG]]
[[Category: signal transduction protein]]
 
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