2chf

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[[Image:2chf.gif|left|200px]]<br /><applet load="2chf" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2chf, resolution 1.8&Aring;" />
 
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'''STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND THE MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS'''<br />
 
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==Overview==
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==STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND THE MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS==
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The response regulator protein of bacterial chemotaxis, CheY, is representative of a large family of signal transduction proteins that function as phosphorylation-activated switches to regulate the activities of associated effector domains. These regulators catalyze the metal ion-dependent phosphoryl transfer and dephosphorylation reactions that control the effector activities. The crystal structures of Salmonella typhimurium CheY with and without Mg2+ bound at the active site have been determined and refined at 1.8-A resolution. While the overall structures of metal-bound and metal-free CheY are similar, significant rearrangements occur within the active site involving the three most highly conserved residues of the response regulator family. Conservation of the cluster of carboxylate side chains at the active site of response regulator domains can be rationalized in terms of their role in coordinating the catalytically essential divalent metal ion. The Mg2+ coordination geometry provides insights to the mechanism of phosphoryl transfer.
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<StructureSection load='2chf' size='340' side='right'caption='[[2chf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2chf]] 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=2CHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CHF FirstGlance]. <br>
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2chf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2chf OCA], [https://pdbe.org/2chf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2chf RCSB], [https://www.ebi.ac.uk/pdbsum/2chf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2chf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/2chf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2chf ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2CHF 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHF OCA].
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis., Stock AM, Martinez-Hackert E, Rasmussen BF, West AH, Stock JB, Ringe D, Petsko GA, Biochemistry. 1993 Dec 14;32(49):13375-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8257674 8257674]
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[[Category: Large Structures]]
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[[Category: Salmonella typhimurium]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Single protein]]
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[[Category: Martinez-Hackert E]]
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[[Category: Martinez-Hackert, E.]]
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[[Category: Petsko G]]
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[[Category: Petsko, G.]]
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[[Category: Rasmussen B]]
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[[Category: Rasmussen, B.]]
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[[Category: Ringe D]]
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[[Category: Ringe, D.]]
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[[Category: Stock A]]
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[[Category: Stock, A.]]
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[[Category: Stock J]]
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[[Category: Stock, J.]]
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[[Category: West A]]
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[[Category: West, A.]]
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[[Category: signal transduction protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:38 2008''
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Current revision

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

PDB ID 2chf

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