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[[Image:2che.png|left|200px]]


{{STRUCTURE_2che| PDB=2che | SCENE= }}
==STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS==
<StructureSection load='2che' size='340' side='right'caption='[[2che]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2che]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CHE 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]] 1.8&#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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2che FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2che OCA], [https://pdbe.org/2che PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2che RCSB], [https://www.ebi.ac.uk/pdbsum/2che PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2che ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CHEY_SALTY CHEY_SALTY] 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. Shows autophosphatase activity which is enhanced by CheZ.
== 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/2che_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=2che ConSurf].
<div style="clear:both"></div>


===STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS===
==See Also==
 
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
{{ABSTRACT_PUBMED_8257674}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
[[2che]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHE OCA].
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
 
[[Category: Martinez-Hackert E]]
==Reference==
[[Category: Petsko G]]
<ref group="xtra">PMID:008257674</ref><references group="xtra"/>
[[Category: Rasmussen B]]
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
[[Category: Ringe D]]
[[Category: Martinez-Hackert, E.]]
[[Category: Stock A]]
[[Category: Petsko, G.]]
[[Category: Stock J]]
[[Category: Rasmussen, B.]]
[[Category: West A]]
[[Category: Ringe, D.]]
[[Category: Stock, A.]]
[[Category: Stock, J.]]
[[Category: West, A.]]
[[Category: Signal transduction protein]]

Latest revision as of 09:17, 14 February 2024

STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS

2che, resolution 1.80Å

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