1f4v

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(New page: 200px<br /><applet load="1f4v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f4v, resolution 2.22&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1f4v.jpg|left|200px]]<br /><applet load="1f4v" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1f4v, resolution 2.22&Aring;" />
 
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'''CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM==
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The chemotactic regulator CheY controls the direction of flagellar, rotation in Escherichia coli. We have determined the crystal structure of, BeF3--activated CheY from E. coli in complex with an N-terminal peptide, derived from its target, FliM. The structure reveals that the first seven, residues of the peptide pack against the beta4-H4 loop and helix H4 of, CheY in an extended conformation, whereas residues 8-15 form two turns of, helix and pack against the H4-beta5-H5 face. The peptide binds the only, region of CheY that undergoes noticeable conformational change upon, activation and would most likely be sandwiched between activated CheY and, the remainder of FliM to reverse the direction of flagellar rotation.
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<StructureSection load='1f4v' size='340' side='right'caption='[[1f4v]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1f4v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F4V 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]] 2.22&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1f4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4v OCA], [https://pdbe.org/1f4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f4v RCSB], [https://www.ebi.ac.uk/pdbsum/1f4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4v ProSAT]</span></td></tr>
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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/f4/1f4v_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=1f4v 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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1F4V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, BEF and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F4V OCA].
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
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==Reference==
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== References ==
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Crystal structure of an activated response regulator bound to its target., Lee SY, Cho HS, Pelton JG, Yan D, Henderson RK, King DS, Huang L, Kustu S, Berry EA, Wemmer DE, Nat Struct Biol. 2001 Jan;8(1):52-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11135671 11135671]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Berry, E.A.]]
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[[Category: Berry EA]]
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[[Category: Cho, H.S.]]
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[[Category: Cho HS]]
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[[Category: Henderson, R.K.]]
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[[Category: Henderson RK]]
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[[Category: Huang, L.S.]]
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[[Category: Huang LS]]
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[[Category: King, D.]]
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[[Category: King D]]
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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: 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: BEF]]
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[[Category: GOL]]
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[[Category: MG]]
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[[Category: bacterial signal transduction]]
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[[Category: bef3]]
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[[Category: peptide-protein complex]]
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[[Category: response regulator]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:37:14 2007''
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Current revision

CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM

PDB ID 1f4v

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