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New page: left|200px<br /><applet load="2chy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2chy, resolution 2.7Å" /> '''THREE-DIMENSIONAL STR...
 
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'''THREE-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXIS'''<br />


==Overview==
==THREE-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXIS==
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.
<StructureSection load='2chy' size='340' side='right'caption='[[2chy]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<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='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>
== 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/2chy_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=2chy ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2CHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CHY OCA].
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 
*[[Receiver domain of sensor histidine kinase CKI1|Receiver domain of sensor histidine kinase CKI1]]
==Reference==
__TOC__
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2645526 2645526]
</StructureSection>
[[Category: Salmonella typhimurium]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Mottonen, J.M.]]
[[Category: Mottonen JM]]
[[Category: Schutt, C.E.]]
[[Category: Schutt CE]]
[[Category: Stock, A.M.]]
[[Category: Stock AM]]
[[Category: Stock, J.B.]]
[[Category: Stock JB]]
[[Category: signal transduction protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:07:45 2007''

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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