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| | <StructureSection load='2fmf' size='340' side='right' caption='[[2fmf]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2fmf' size='340' side='right' caption='[[2fmf]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fmf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FMF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fmf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FMF FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fka|2fka]], [[2flk|2flk]], [[2fmh|2fmh]], [[2fmi|2fmi]], [[2fmk|2fmk]]</td></tr> | | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fka|2fka]], [[2flk|2flk]], [[2fmh|2fmh]], [[2fmi|2fmi]], [[2fmk|2fmk]]</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cheY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cheY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fmf RCSB], [http://www.ebi.ac.uk/pdbsum/2fmf PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmf OCA], [http://pdbe.org/2fmf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fmf RCSB], [http://www.ebi.ac.uk/pdbsum/2fmf PDBsum]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2fmf" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | + | [[Category: Salty]] |
| | [[Category: Guhaniyogi, J]] | | [[Category: Guhaniyogi, J]] |
| | [[Category: Robinson, V L]] | | [[Category: Robinson, V L]] |
| Structural highlights
Function
[CHEY_SALTY] 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. Shows autophosphatase activity which is enhanced by CheZ. [CHEZ_SALTY] Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). Acts on free CheY-P.[1] [2] [3] [4] [5]
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
Chemotaxis, the environment-specific swimming behavior of a bacterial cell is controlled by flagellar rotation. The steady-state level of the phosphorylated or activated form of the response regulator CheY dictates the direction of flagellar rotation. CheY phosphorylation is regulated by a fine equilibrium of three phosphotransfer activities: phosphorylation by the kinase CheA, its auto-dephosphorylation and dephosphorylation by its phosphatase CheZ. Efficient dephosphorylation of CheY by CheZ requires two spatially distinct protein-protein contacts: tethering of the two proteins to each other and formation of an active site for dephosphorylation. The former involves interaction of phosphorylated CheY with the small highly conserved C-terminal helix of CheZ (CheZ(C)), an indispensable structural component of the functional CheZ protein. To understand how the CheZ(C) helix, representing less than 10% of the full-length protein, ascertains molecular specificity of binding to CheY, we have determined crystal structures of CheY in complex with a synthetic peptide corresponding to 15 C-terminal residues of CheZ (CheZ(200-214)) at resolutions ranging from 2.0 A to 2.3A. These structures provide a detailed view of the CheZ(C) peptide interaction both in the presence and absence of the phosphoryl analog, BeF3-. Our studies reveal that two different modes of binding the CheZ(200-214) peptide are dictated by the conformational state of CheY in the complex. Our structures suggest that the CheZ(C) helix binds to a "meta-active" conformation of inactive CheY and it does so in an orientation that is distinct from the one in which it binds activated CheY. Our dual binding mode hypothesis provides implications for reverse information flow in CheY and extends previous observations on inherent resilience in CheY-like signaling domains.
Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation.,Guhaniyogi J, Robinson VL, Stock AM J Mol Biol. 2006 Jun 9;359(3):624-45. Epub 2006 Apr 6. PMID:16674976[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lukat GS, Lee BH, Mottonen JM, Stock AM, Stock JB. Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis. J Biol Chem. 1991 May 5;266(13):8348-54. PMID:1902474
- ↑ Huang C, Stewart RC. CheZ mutants with enhanced ability to dephosphorylate CheY, the response regulator in bacterial chemotaxis. Biochim Biophys Acta. 1993 Oct 6;1202(2):297-304. PMID:8399392
- ↑ Bren A, Welch M, Blat Y, Eisenbach M. Signal termination in bacterial chemotaxis: CheZ mediates dephosphorylation of free rather than switch-bound CheY. Proc Natl Acad Sci U S A. 1996 Sep 17;93(19):10090-3. PMID:8816756
- ↑ Blat Y, Gillespie B, Bren A, Dahlquist FW, Eisenbach M. Regulation of phosphatase activity in bacterial chemotaxis. J Mol Biol. 1998 Dec 11;284(4):1191-9. PMID:9837737 doi:http://dx.doi.org/10.1006/jmbi.1998.2224
- ↑ Wolanin PM, Webre DJ, Stock JB. Mechanism of phosphatase activity in the chemotaxis response regulator CheY. Biochemistry. 2003 Dec 2;42(47):14075-82. PMID:14636076 doi:http://dx.doi.org/10.1021/bi034883t
- ↑ Guhaniyogi J, Robinson VL, Stock AM. Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation. J Mol Biol. 2006 Jun 9;359(3):624-45. Epub 2006 Apr 6. PMID:16674976 doi:http://dx.doi.org/10.1016/j.jmb.2006.03.050
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