1cey

<StructureSection load='1cey' size='340' side='right'caption='[[1cey]], [[NMR_Ensembles_of_Models | 46 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1cey]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEY FirstGlance]. <br>

</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=1cey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cey OCA], [https://pdbe.org/1cey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cey RCSB], [https://www.ebi.ac.uk/pdbsum/1cey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cey ProSAT]</span></td></tr>

[[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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== Publication Abstract from PubMed ==

NMR spectroscopy has been used to study recombinant Escherichia coli CheY, a 128-residue protein involved in regulating bacterial chemotaxis. Heteronuclear three- and four-dimensional (3D and 4D) experiments have provided sequence-specific resonance assignments and quantitation of short-, medium-, and long-range distance restraints from nuclear Overhauser enhancement (NOE) intensities. These distance restraints were further supplemented with measurements of three-bond scalar coupling constants to define the local dihedral angles, and with the identification of amide protons undergoing slow solvent exchange from which hydrogen-bonding patterns were identified. The current model structure shows the same global fold of CheY as existing X-ray structures (Volz &amp; Matsumura, 1991; Stock et al. 1993) with a (beta/alpha)5 motif of five parallel beta-strands at the central core surrounded by three alpha-helices on one face and with two on the opposite side. Heteronuclear 15N-1H relaxation experiments are interpreted to show portions of the protein structure in the Mg2+ binding loop are ill-defined because of slow motion (chemical exchange) on the NMR time scale. Moreover, the presence of Mg2+ disrupts the salt bridge between the highly conserved Lys-109 and Asp-57, the site of phosphorylation.

Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy.,Moy FJ, Lowry DF, Matsumura P, Dahlquist FW, Krywko JE, Domaille PJ Biochemistry. 1994 Sep 6;33(35):10731-42. PMID:8075074<ref>PMID:8075074</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1cey" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: Dahlquist, F W]]

[[Category: Domaille, P J]]

[[Category: Krywko, J E]]

[[Category: Lowry, D F]]

[[Category: Matsumura, P]]

[[Category: Moy, F J]]

[[Category: Signal transduction]]