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1djm

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{{Seed}}
 
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[[Image:1djm.png|left|200px]]
 
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==SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI==
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The line below this paragraph, containing "STRUCTURE_1djm", creates the "Structure Box" on the page.
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<StructureSection load='1djm' size='340' side='right'caption='[[1djm]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1djm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DJM FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1djm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1djm OCA], [https://pdbe.org/1djm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1djm RCSB], [https://www.ebi.ac.uk/pdbsum/1djm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1djm ProSAT]</span></td></tr>
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{{STRUCTURE_1djm| PDB=1djm | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CHEY_ECOLI CHEY_ECOLI] 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. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator.<ref>PMID:20346719</ref>
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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/dj/1djm_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=1djm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The CheY protein is the response regulator in bacterial chemotaxis. Phosphorylation of a conserved aspartyl residue induces structural changes that convert the protein from an inactive to an active state. The short half-life of the aspartyl-phosphate has precluded detailed structural analysis of the active protein. Persistent activation of Escherichia coli CheY was achieved by complexation with beryllofluoride (BeF(3)(-)) and the structure determined by NMR spectroscopy to a backbone r.m.s.d. of 0.58(+/-0.08) A. Formation of a hydrogen bond between the Thr87 OH group and an active site acceptor, presumably Asp57.BeF(3)(-), stabilizes a coupled rearrangement of highly conserved residues, Thr87 and Tyr106, along with displacement of beta4 and H4, to yield the active state. The coupled rearrangement may be a more general mechanism for activation of receiver domains.
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===SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI===
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NMR structure of activated CheY.,Cho HS, Lee SY, Yan D, Pan X, Parkinson JS, Kustu S, Wemmer DE, Pelton JG J Mol Biol. 2000 Mar 31;297(3):543-51. PMID:10731410<ref>PMID:10731410</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1djm" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10731410}}, adds the Publication Abstract to the page
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10731410 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10731410}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1DJM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJM OCA].
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==Reference==
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NMR structure of activated CheY., Cho HS, Lee SY, Yan D, Pan X, Parkinson JS, Kustu S, Wemmer DE, Pelton JG, J Mol Biol. 2000 Mar 31;297(3):543-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10731410 10731410]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cho, H S.]]
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[[Category: Cho HS]]
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[[Category: Kustu, S.]]
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[[Category: Kustu S]]
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[[Category: Lee, S Y.]]
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[[Category: Lee SY]]
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[[Category: Pan, X.]]
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[[Category: Pan X]]
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[[Category: Parkinson, J S.]]
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[[Category: Parkinson JS]]
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[[Category: Pelton, J G.]]
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[[Category: Pelton JG]]
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[[Category: Wemmer, D E.]]
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[[Category: Wemmer DE]]
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[[Category: Yan, D.]]
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[[Category: Yan D]]
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[[Category: Befx]]
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[[Category: Chemotaxis]]
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[[Category: Chey]]
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[[Category: Response regulator]]
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[[Category: Two-component]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:09:56 2008''
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Current revision

SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI

PDB ID 1djm

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