1ffs

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(New page: 200px<br /><applet load="1ffs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ffs, resolution 2.4&Aring;" /> '''CHEY-BINDING DOMAIN O...)
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[[Image:1ffs.jpg|left|200px]]<br /><applet load="1ffs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ffs, resolution 2.4&Aring;" />
 
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'''CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM CRYSTALS SOAKED IN ACETYL PHOSPHATE'''<br />
 
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==Overview==
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==CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM CRYSTALS SOAKED IN ACETYL PHOSPHATE==
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New crystallographic structures of the response regulator CheY in, association with CheA(124--257), its binding domain in the kinase CheA, have been determined. In all crystal forms, the molecular interactions at, the heterodimer interface are identical. Soaking experiments have been, performed on the crystals using acetyl phosphate as phosphodonor to CheY., No phosphoryl group attached to Asp57 of CheY is visible from the electron, density, but the response regulator in the CheY-CheA(124--257) complex may, have undergone a phosphorylation-dephosphorylation process. The, distribution of water molecules and the geometry of the active site have, changed and are now similar to those of isolated CheY. In a second soaking, experiment, imido-diphosphate, an inhibitor of the phosphorylation, reaction, was used. This compound binds in the vicinity of the active, site, close to the N-terminal part of the first alpha-helix. Together, these results suggest that the binding of CheY to CheA(124--257) generates, a geometry of the active site that favours phosphorylation and that, imido-diphosphate interferes with phosphorylation by precluding structural, changes in this region.
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<StructureSection load='1ffs' size='340' side='right'caption='[[1ffs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ffs]] is a 4 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=1FFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FFS 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]] 2.4&#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=MN:MANGANESE+(II)+ION'>MN</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=1ffs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffs OCA], [https://pdbe.org/1ffs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ffs RCSB], [https://www.ebi.ac.uk/pdbsum/1ffs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ffs 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/ff/1ffs_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=1ffs 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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1FFS 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 MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FFS OCA].
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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== References ==
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==Reference==
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<references/>
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Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY--CheA(124--257) complex., Gouet P, Chinardet N, Welch M, Guillet V, Cabantous S, Birck C, Mourey L, Samama JP, Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):44-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11134926 11134926]
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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: Birck, C.]]
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[[Category: Birck C]]
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[[Category: Chinardet, N.]]
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[[Category: Chinardet N]]
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[[Category: Gouet, P.]]
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[[Category: Gouet P]]
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[[Category: Guillet, V.]]
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[[Category: Guillet V]]
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[[Category: Mourey, L.]]
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[[Category: Mourey L]]
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[[Category: Samama, J.P.]]
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[[Category: Samama J-P]]
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[[Category: Welch, M.]]
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[[Category: Welch M]]
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[[Category: MN]]
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[[Category: doubly wound (beta/alpha)5 fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:53:29 2007''
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Current revision

CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM CRYSTALS SOAKED IN ACETYL PHOSPHATE

PDB ID 1ffs

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