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==THREE-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXIS==
==THREE-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXIS==
<StructureSection load='2chy' size='340' side='right' caption='[[2chy]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='2chy' size='340' side='right'caption='[[2chy]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2chy]] 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=2CHY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHY FirstGlance]. <br>
<table><tr><td colspan='2'>[[2chy]] 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=2CHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CHY FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2chy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2chy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2chy RCSB], [http://www.ebi.ac.uk/pdbsum/2chy PDBsum]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#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=2chy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2chy OCA], [https://pdbe.org/2chy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2chy RCSB], [https://www.ebi.ac.uk/pdbsum/2chy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2chy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/2chy_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/2chy_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata 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=2chy ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Homologies among bacterial signal transduction proteins suggest that a common mechanism mediates processes such as chemotaxis, osmoregulation, sporulation, virulence, and responses to nitrogen, phosphorous and oxygen deprivation. A common kinase-mediated phosphotransfer reaction has recently been identified in chemotaxis, nitrogen regulation, and osmoregulation. In chemotaxis, the CheA kinase passes a phosphoryl group to the cytoplasmic protein CheY, which functions as a phosphorylation-activated switch that interacts with flagellar components to regulate motility. We report here the X-ray crystal structure of the Salmonella typhimurium CheY protein. The determination of the structure was facilitated by the use of site-specific mutagenesis to engineer heavy-atom binding sites. CheY is a single-domain protein composed of a doubly wound five-stranded parallel beta-sheet. The phosphoacceptor site in CheY is probably a cluster of aspartic-acid side chains near the C-terminal edge of the beta-sheet. The pattern of sequence similarity of CheY with components of other regulatory systems can be interpreted in the light of the CheY structure and supports the view that this family of proteins have a common structural motif and active site.
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis.,Stock AM, Mottonen JM, Stock JB, Schutt CE Nature. 1989 Feb 23;337(6209):745-9. PMID:2645526<ref>PMID:2645526</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Chemotaxis protein|Chemotaxis protein]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
*[[Receiver domain of sensor histidine kinase CKI1|Receiver domain of sensor histidine kinase CKI1]]
*[[Receiver domain of sensor histidine kinase CKI1|Receiver domain of sensor histidine kinase CKI1]]
*[[Response regulator|Response regulator]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
[[Category: Large Structures]]
[[Category: Mottonen, J M]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Schutt, C E]]
[[Category: Mottonen JM]]
[[Category: Stock, A M]]
[[Category: Schutt CE]]
[[Category: Stock, J B]]
[[Category: Stock AM]]
[[Category: Signal transduction protein]]
[[Category: Stock JB]]

Latest revision as of 12:18, 14 February 2024

THREE-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXISTHREE-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXIS

Structural highlights

2chy is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2chy, resolution 2.70Å

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