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| | <StructureSection load='1e6l' size='340' side='right'caption='[[1e6l]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1e6l' size='340' side='right'caption='[[1e6l]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1e6l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E6L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1e6l]] is a 1 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=1E6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E6L FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1udr|1udr]], [[1eay|1eay]], [[1c4w|1c4w]], [[1bdj|1bdj]], [[1ab5|1ab5]], [[1ab6|1ab6]], [[1a0o|1a0o]], [[1e6k|1e6k]], [[1e6m|1e6m]], [[3chy|3chy]], [[5chy|5chy]], [[6chy|6chy]], [[1chn|1chn]], [[1cey|1cey]], [[1ymu|1ymu]], [[1ymv|1ymv]], [[1cye|1cye]], [[1vlz|1vlz]], [[1ehc|1ehc]], [[1hey|1hey]], [[1d4z|1d4z]], [[1djm|1djm]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cheY, b1882, JW1871 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1e6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e6l OCA], [https://pdbe.org/1e6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e6l RCSB], [https://www.ebi.ac.uk/pdbsum/1e6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e6l ProSAT]</span></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=1e6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e6l OCA], [https://pdbe.org/1e6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e6l RCSB], [https://www.ebi.ac.uk/pdbsum/1e6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e6l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Coll, M]] | + | [[Category: Coll M]] |
| - | [[Category: Cronet, P]] | + | [[Category: Cronet P]] |
| - | [[Category: Lacroix, E]] | + | [[Category: Lacroix E]] |
| - | [[Category: Lopez-Hernandez, E]] | + | [[Category: Lopez-Hernandez E]] |
| - | [[Category: Parraga, A]] | + | [[Category: Parraga A]] |
| - | [[Category: Serrano, L]] | + | [[Category: Serrano L]] |
| - | [[Category: Sola, M]] | + | [[Category: Sola M]] |
| - | [[Category: Active site mutant]]
| + | |
| - | [[Category: Chemotaxis]]
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| - | [[Category: Signaling protein]]
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| - | [[Category: Two-component signal transduction system]]
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| Structural highlights
Function
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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The signal transduction protein CheY displays an alpha/beta-parallel polypeptide folding, including a highly unstable helix alpha4 and a strongly charged active site. Helix alpha4 has been shown to adopt various positions and conformations in different crystal structures, suggesting that it is a mobile segment. Furthermore, the instability of this helix is believed to have functional significance because it is involved in protein-protein contacts with the transmitter protein kinase CheA, the target protein FliM and the phosphatase CheZ. The active site of CheY comprises a cluster of three aspartic acid residues and a lysine residue, all of which participate in the binding of the Mg(2+) needed for the protein activation. Two steps were followed to study the activation mechanism of CheY upon phosphorylation: first, we independently substituted the three aspartic acid residues in the active site with alanine; second, several mutations were designed in helix alpha 4, both to increase its level of stability and to improve its packing against the protein core. The structural and thermodynamic analysis of these mutant proteins provides further evidence of the connection between the active-site area and helix alpha 4, and helps to understand how small movements at the active site are transmitted and amplified to the protein surface.
Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY.,Sola M, Lopez-Hernandez E, Cronet P, Lacroix E, Serrano L, Coll M, Parraga A J Mol Biol. 2000 Oct 20;303(2):213-25. PMID:11023787[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Paul K, Nieto V, Carlquist WC, Blair DF, Harshey RM. The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism. Mol Cell. 2010 Apr 9;38(1):128-39. doi: 10.1016/j.molcel.2010.03.001. Epub 2010, Mar 25. PMID:20346719 doi:10.1016/j.molcel.2010.03.001
- ↑ Sola M, Lopez-Hernandez E, Cronet P, Lacroix E, Serrano L, Coll M, Parraga A. Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY. J Mol Biol. 2000 Oct 20;303(2):213-25. PMID:11023787 doi:10.1006/jmbi.2000.4507
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