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[[Image:2pmc.jpg|left|200px]]<br /><applet load="2pmc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2pmc, resolution 2.688&Aring;" />
'''Crystal Structure of CheY-Mg(2+) in Complex with CheZ(C15) Peptide solved from a P1 Crystal'''<br />


==Overview==
==Crystal Structure of CheY-Mg(2+) in Complex with CheZ(C15) Peptide solved from a P1 Crystal==
Chemotaxis, a means for motile bacteria to sense the environment and, achieve directed swimming, is controlled by flagellar rotation. The, primary output of the chemotaxis machinery is the phosphorylated form of, the response regulator CheY (P approximately CheY). The steady-state level, of P approximately CheY dictates the direction of rotation of the, flagellar motor. The chemotaxis signal in the form of P approximately CheY, is terminated by the phosphatase CheZ. Efficient dephosphorylation of CheY, by CheZ requires two distinct protein-protein interfaces: one involving, the strongly conserved C-terminal helix of CheZ (CheZC) tethering the two, proteins together and the other constituting an active site for catalytic, dephosphorylation. In a previous work (Guhaniyogi J., Robinson V. L. and, Stock A. M. 2006. J. Mol. Biol. 359: 624-645), we presented, high-resolution crystal structures of CheY in complex with the CheZC, peptide that revealed alternate binding modes subject to the, conformational state of CheY. In this study, we report biochemical and, structural data that support the alternate binding mode hypothesis and, identify key recognition elements in the CheY-CheZC interaction. In, addition, we present kinetic studies of CheZC-associated effect on CheY, phosphorylation with its physiologically relevant phosphodonor, the, histidine kinase CheA. Our results indicate mechanistic differences in, phosphotransfer from the kinase CheA versus from small molecule, phosphodonors explaining a modest 2-fold increase of CheY phosphorylation, with the former, observed in this study, relative to a 10-fold increase, previously documented with the latter.
<StructureSection load='2pmc' size='340' side='right'caption='[[2pmc]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2pmc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PMC 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]] 2.688&#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=2pmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pmc OCA], [https://pdbe.org/2pmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pmc RCSB], [https://www.ebi.ac.uk/pdbsum/2pmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pmc 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/pm/2pmc_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=2pmc ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2PMC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+201'>AC1</scene> and <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+202'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PMC OCA].
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Interaction of CheY with the C-Terminal Peptide of CheZ., Guhaniyogi J, Wu T, Patel SS, Stock AM, J Bacteriol. 2007 Dec 14;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18083806 18083806]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
[[Category: Salmonella typhimurium]]
[[Category: Guhaniyogi J]]
[[Category: Guhaniyogi, J.]]
[[Category: Stock AM]]
[[Category: Stock, A.M.]]
[[Category: MG]]
[[Category: chemotaxis]]
[[Category: chey-chez peptide complex]]
[[Category: signaling protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:18:03 2008''

Latest revision as of 12:10, 21 February 2024

Crystal Structure of CheY-Mg(2+) in Complex with CheZ(C15) Peptide solved from a P1 CrystalCrystal Structure of CheY-Mg(2+) in Complex with CheZ(C15) Peptide solved from a P1 Crystal

Structural highlights

2pmc is a 6 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.688Å
Ligands:
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

2pmc, resolution 2.69Å

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