1ehc: Difference between revisions

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


{{Structure
==STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN CHEY==
|PDB= 1ehc |SIZE=350|CAPTION= <scene name='initialview01'>1ehc</scene>, resolution 2.26&Aring;
<StructureSection load='1ehc' size='340' side='right'caption='[[1ehc]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ehc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ehc OCA], [http://www.ebi.ac.uk/pdbsum/1ehc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ehc RCSB]</span>
== 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 ==
'''STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN CHEY'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eh/1ehc_consurf.spt"</scriptWhenChecked>
An aspartate to lysine mutation at position 13 of the chemotaxis regulatory protein CheY causes a constitutive tumbly phenotype when expressed at high copy number in vivo even though the mutant protein is not phosphorylatable. These properties suggest that the D13K mutant adopts the active, signaling conformation of CheY independent of phosphorylation, so knowledge of its structure could explain the activation mechanism of CheY. The x-ray crystallographic structure of the CheY D13K mutant has been solved and refined at 2.3 A resolution to an R-factor of 14.3%. The mutant molecule shows no significant differences in backbone conformation when compared with the wild-type, Mg2+-free structure, but there are localized changes within the active site. The side chain of lysine 13 blocks access to the active site, whereas its epsilon-amino group has no bonding interactions with other groups in the region. Also in the active site, the bond between lysine 109 and aspartate 57 is weakened, and the solvent structure is perturbed. Although the D13K mutant has the inactive conformation in the crystalline form, rearrangements in the active site appear to weaken the overall structure of that region, potentially creating a metastable state of the molecule. If a conformational change is required for signaling by CheY D13K, then it most likely proceeds dynamically, in solution.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==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 Sun Mar 30 20:02:38 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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