1cey
From Proteopedia
(Difference between revisions)
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==ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF CHEMOTAXIS Y PROTEIN USING THREE-AND FOUR-DIMENSIONAL HETERONUCLEAR (13C,15N) NMR SPECTROSCOPY== | ==ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF CHEMOTAXIS Y PROTEIN USING THREE-AND FOUR-DIMENSIONAL HETERONUCLEAR (13C,15N) NMR SPECTROSCOPY== | ||
- | <StructureSection load='1cey' size='340' side='right' caption='[[1cey]], [[NMR_Ensembles_of_Models | 46 NMR models]]' scene=''> | + | <StructureSection load='1cey' size='340' side='right'caption='[[1cey]], [[NMR_Ensembles_of_Models | 46 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cey]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CEY FirstGlance]. <br> | <table><tr><td colspan='2'>[[1cey]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cey OCA], [http://pdbe.org/1cey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cey RCSB], [http://www.ebi.ac.uk/pdbsum/1cey PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cey ProSAT]</span></td></tr> | </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=1cey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cey OCA], [http://pdbe.org/1cey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cey RCSB], [http://www.ebi.ac.uk/pdbsum/1cey PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cey ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | {{Large structure}} | ||
== Function == | == Function == | ||
[[http://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> | [[http://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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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ce/1cey_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ce/1cey_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Dahlquist, F W]] | [[Category: Dahlquist, F W]] | ||
[[Category: Domaille, P J]] | [[Category: Domaille, P J]] |
Revision as of 07:13, 29 May 2019
ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF CHEMOTAXIS Y PROTEIN USING THREE-AND FOUR-DIMENSIONAL HETERONUCLEAR (13C,15N) NMR SPECTROSCOPY
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