1ehc: Difference between revisions

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[[Image:1ehc.png|left|200px]]


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==STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN CHEY==
The line below this paragraph, containing "STRUCTURE_1ehc", creates the "Structure Box" on the page.
<StructureSection load='1ehc' size='340' side='right'caption='[[1ehc]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ehc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EHC 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]] 2.26&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1ehc|  PDB=1ehc  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ehc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ehc OCA], [https://pdbe.org/1ehc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ehc RCSB], [https://www.ebi.ac.uk/pdbsum/1ehc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ehc ProSAT]</span></td></tr>
 
</table>
===STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN CHEY===
== 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>
 
== Evolutionary Conservation ==
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Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eh/1ehc_consurf.spt"</scriptWhenChecked>
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==About this Structure==
  </jmolCheckbox>
1EHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHC OCA].  
</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=1ehc ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheY., Jiang M, Bourret RB, Simon MI, Volz K, J Biol Chem. 1997 May 2;272(18):11850-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9115243 9115243]
<references/>
[[Category: Escherichia coli]]
__TOC__
[[Category: Single protein]]
</StructureSection>
[[Category: Bourret, R.]]
[[Category: Escherichia coli K-12]]
[[Category: Jiang, M.]]
[[Category: Large Structures]]
[[Category: Simon, M.]]
[[Category: Bourret R]]
[[Category: Volz, K.]]
[[Category: Jiang M]]
[[Category: Chemotaxis]]
[[Category: Simon M]]
[[Category: Chey]]
[[Category: Volz K]]
[[Category: Flagellar rot]]
[[Category: Phosphorylation]]
[[Category: Response regulator]]
[[Category: Sensory transduction]]
[[Category: Signal transduction]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:42:06 2008''

Latest revision as of 10:02, 7 February 2024

STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN CHEYSTRUCTURE OF SIGNAL TRANSDUCTION PROTEIN CHEY

Structural highlights

1ehc is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.26Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

References

  1. ↑ 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

1ehc, resolution 2.26Å

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