2pmc: Difference between revisions

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-[[Image:2pmc.jpg|left|200px]]
- {{Structure
+==Crystal Structure of CheY-Mg(2+) in Complex with CheZ(C15) Peptide solved from a P1 Crystal==
-|PDB= 2pmc |SIZE=350|CAPTION= <scene name='initialview01'>2pmc</scene>, resolution 2.688&Aring;
+<StructureSection load='2pmc' size='340' side='right'caption='[[2pmc]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
-|SITE= <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>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
+<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>
-|ACTIVITY=
+</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>
-|GENE= cheY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium])
+<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>
-'''Crystal Structure of CheY-Mg(2+) in Complex with CheZ(C15) Peptide solved from a P1 Crystal'''
+==See Also==
+*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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-CheY). The steady-state level of P-CheY dictates the direction of rotation of the flagellar motor. The chemotaxis signal in the form of P-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 (CheZ(C)) tethering the two proteins together and the other constituting an active site for catalytic dephosphorylation. In a previous work (J. Guhaniyogi, V. L. Robinson, and A. M. Stock, J. Mol. Biol. 359:624-645, 2006), we presented high-resolution crystal structures of CheY in complex with the CheZ(C) 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-CheZ(C) interaction. In addition, we present kinetic studies of the CheZ(C)-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 that from small-molecule phosphodonors, explaining a modest twofold increase of CheY phosphorylation with the former, observed in this study, relative to a 10-fold increase previously documented with the latter.
+[[Category: Large Structures]]
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
-==About this Structure==
+[[Category: Guhaniyogi J]]
-PMC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PMC OCA].
+[[Category: Stock AM]]
-==Reference==
-Interaction of CheY with the C-terminal peptide of CheZ., Guhaniyogi J, Wu T, Patel SS, Stock AM, J Bacteriol. 2008 Feb;190(4):1419-28. Epub 2007 Dec 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18083806 18083806]
-[[Category: Protein complex]]
-[[Category: Salmonella typhimurium]]
-[[Category: Guhaniyogi, J.]]
-[[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 Thu Mar 20 18:14:48 2008''