1fqw: Difference between revisions

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New page: left|200px<br /><applet load="1fqw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fqw, resolution 2.37Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1fqw.gif|left|200px]]<br /><applet load="1fqw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fqw, resolution 2.37&Aring;" />
'''CRYSTAL STRUCTURE OF ACTIVATED CHEY'''<br />


==Overview==
==CRYSTAL STRUCTURE OF ACTIVATED CHEY==
The crystal structure of BeF(3)(-)-activated CheY, with manganese in the, magnesium binding site, was determined at 2.4-A resolution. BeF(3)(-), bonds to Asp(57), the normal site of phosphorylation, forming a hydrogen, bond and salt bridge with Thr(87) and Lys(109), respectively. The six, coordination sites for manganese are satisfied by a fluorine of BeF(3)(-), the side chain oxygens of Asp(13) and Asp(57), the carbonyl oxygen of, Asn(59), and two water molecules. All of the active site interactions seen, for BeF(3)(-)-CheY are also observed in P-Spo0A(r). Thus, BeF(3)(-), activates CheY as well as other receiver domains by mimicking both the, tetrahedral geometry and electrostatic potential of a phosphoryl group., The aromatic ring of Tyr(106) is found buried within a hydrophobic pocket, formed by beta-strand beta4 and helix H4. The tyrosine side chain is, stabilized in this conformation by a hydrogen bond between the hydroxyl, group and the backbone carbonyl oxygen of Glu(89). This hydrogen bond, appears to stabilize the active conformation of the beta4/H4 loop., Comparison of the backbone coordinates for the active and inactive states, of CheY reveals that only modest changes occur upon activation, except in, the loops, with the largest changes occurring in the beta4/H4 loop. This, region is known to be conformationally flexible in inactive CheY and is, part of the surface used by activated CheY for binding its target, FliM., The pattern of activation-induced backbone coordinate changes is similar, to that seen in FixJ(r). A common feature in the active sites of, BeF(3)(-)-CheY, P-Spo0A(r), P-FixJ(r), and phosphono-CheY is a salt bridge, between Lys(109) Nzeta and the phosphate or its equivalent, beryllofluoride. This suggests that, in addition to the concerted, movements of Thr(87) and Tyr(106) (Thr-Tyr coupling), formation of the, Lys(109)-PO(3)(-) salt bridge is directly involved in the activation of, receiver domains generally.
<StructureSection load='1fqw' size='340' side='right'caption='[[1fqw]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fqw]] is a 2 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=1FQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.37&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=1fqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqw OCA], [https://pdbe.org/1fqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqw RCSB], [https://www.ebi.ac.uk/pdbsum/1fqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqw ProSAT]</span></td></tr>
</table>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/1fqw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1fqw ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN and BEF as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FQW OCA].
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structure of activated CheY. Comparison with other activated receiver domains., Lee SY, Cho HS, Pelton JG, Yan D, Berry EA, Wemmer DE, J Biol Chem. 2001 May 11;276(19):16425-31. Epub 2001 Feb 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11279165 11279165]
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berry, E.A.]]
[[Category: Berry EA]]
[[Category: Cho, H.S.]]
[[Category: Cho HS]]
[[Category: Lee, S.Y.]]
[[Category: Lee SY]]
[[Category: Pelton, J.G.]]
[[Category: Pelton JG]]
[[Category: Wemmer, D.E.]]
[[Category: Wemmer DE]]
[[Category: Yan, D.]]
[[Category: Yan D]]
[[Category: BEF]]
[[Category: MN]]
[[Category: activated chey]]
[[Category: bef3]]
[[Category: chemotaxis]]
[[Category: receiver domain]]
[[Category: response regulator]]
[[Category: two-component signal transduction]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:10:32 2007''

Latest revision as of 10:18, 7 February 2024

CRYSTAL STRUCTURE OF ACTIVATED CHEYCRYSTAL STRUCTURE OF ACTIVATED CHEY

Structural highlights

1fqw is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.37Å
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.

See Also

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

1fqw, resolution 2.37Å

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