3ffw - Revision history

OCA at 09:49, 21 February 2024

OCA — Wed, 21 Feb 2024 09:49:19 GMT

←Older revision		Revision as of 09:49, 21 February 2024
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	<StructureSection load='3ffw' size='340' side='right'caption='[[3ffw]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3ffw' size='340' side='right'caption='[[3ffw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ffw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FFW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ffw]] is a 2 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=3FFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FFW FirstGlance]. <br>
-	</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3f7n\|3f7n]], [[3fft\|3fft]], [[3ffx\|3ffx]]</div></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1882, cheY, JW1871 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])~~</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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [https://pdbe.org/3ffw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [https://www.ebi.ac.uk/pdbsum/3ffw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffw ProSAT]</span></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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [https://pdbe.org/3ffw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [https://www.ebi.ac.uk/pdbsum/3ffw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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>	+	[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 ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=3ffw ConSurf].		</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=3ffw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	In two-component regulatory systems, covalent phosphorylation typically activates the response regulator signaling protein, and hydrolysis of the phosphoryl group reestablishes the inactive state. Despite highly conserved three-dimensional structures and active-site features, the rates of catalytic autodephosphorylation for different response regulators vary by a factor of almost 10(6). Previous studies identified two variable active-site residues, corresponding to Escherichia coli CheY residues 59 and 89, that modulate response regulator autodephosphorylation rates about 100-fold. Here, a set of five CheY mutants, which match other "model" response regulators (ArcA, CusR, DctD, FixJ, PhoB, or Spo0F) at variable active-site positions corresponding to CheY residues 14, 59, and 89, were characterized functionally and structurally in an attempt to identify mechanisms that modulate autodephosphorylation rate. As expected, the autodephosphorylation rates of the CheY mutants were reduced 6- to 40-fold relative to wild-type CheY, but all still autodephosphorylated 12- to 80-fold faster than their respective model response regulators. Comparison of X-ray crystal structures of the five CheY mutants (complexed with the phosphoryl group analogue BeF(3)(-)) to wild-type CheY or corresponding model response regulator structures gave strong evidence for steric obstruction of the phosphoryl group from the attacking water molecule as one mechanism to enhance phosphoryl group stability. Structural data also suggested that impeding the change of a response regulator from the active to the inactive conformation might retard the autodephosphorylation reaction if the two processes are coupled, and that the residue at position '58' may contribute to rate modulation. A given combination of amino acids at positions '14', '59', and '89' adopted similar conformations regardless of protein context (CheY or model response regulator), suggesting that knowledge of residue identity may be sufficient to predict autodephosphorylation rate, and hence the kinetics of the signaling response, in the response regulator family of proteins.
-
-	Matching biochemical reaction kinetics to the timescales of life: structural determinants that influence the autodephosphorylation rate of response regulator proteins.,Pazy Y, Wollish AC, Thomas SA, Miller PJ, Collins EJ, Bourret RB, Silversmith RE J Mol Biol. 2009 Oct 9;392(5):1205-20. Epub 2009 Jul 28. PMID:19646451<ref>PMID:19646451</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3ffw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bourret~~, R B~~]]	+	[[Category: Bourret RB]]
-	[[Category: Collins~~, E J~~]]	+	[[Category: Collins EJ]]
-	[[Category: Pazy, Y]]	+	[[Category: Pazy Y]]
-	~~[[Category: Bef3]]~~	+
-	~~[[Category: Chemotaxis]]~~	+
-	~~[[Category: Flagellar rotation]]~~	+
-	~~[[Category: Magnesium]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Receiver domain]]~~	+
-	~~[[Category: Response regulator]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Two-component regulatory system]]~~	+
-	~~[[Category: Two-component signal transduction~~]]	+

OCA at 19:53, 20 October 2021

OCA — Wed, 20 Oct 2021 19:53:52 GMT

←Older revision		Revision as of 19:53, 20 October 2021
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	==Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+==		==Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+==
-	<StructureSection load='3ffw' size='340' side='right' caption='[[3ffw]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='3ffw' size='340' side='right'caption='[[3ffw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ffw]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3FFW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ffw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FFW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <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" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <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">[[3f7n\|3f7n]], [[3fft\|3fft]], [[3ffx\|3ffx]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3f7n\|3f7n]], [[3fft\|3fft]], [[3ffx\|3ffx]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1882, cheY, JW1871 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1882, cheY, JW1871 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [~~http~~://pdbe.org/3ffw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3ffw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffw ProSAT]</span></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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [https://pdbe.org/3ffw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [https://www.ebi.ac.uk/pdbsum/3ffw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffw ProSAT]</span></td></tr>
	</table>		</table>
	== 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>	+	[[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 ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/3ffw_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/3ffw_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>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 3ffw" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3ffw" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Chemotaxis protein 3D structures\|Chemotaxis protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Ecoli]]		[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: Bourret, R B]]		[[Category: Bourret, R B]]
	[[Category: Collins, E J]]		[[Category: Collins, E J]]

OCA at 06:41, 1 November 2017

OCA — Wed, 01 Nov 2017 06:41:20 GMT

←Older revision		Revision as of 06:41, 1 November 2017
Line 1:		Line 1:
		+
	==Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+==		==Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+==
	<StructureSection load='3ffw' size='340' side='right' caption='[[3ffw]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3ffw' size='340' side='right' caption='[[3ffw]], [[Resolution\|resolution]] 2.00Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3f7n\|3f7n]], [[3fft\|3fft]], [[3ffx\|3ffx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3f7n\|3f7n]], [[3fft\|3fft]], [[3ffx\|3ffx]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1882, cheY, JW1871 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1882, cheY, JW1871 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [http://pdbe.org/3ffw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [http://www.ebi.ac.uk/pdbsum/3ffw 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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [http://pdbe.org/3ffw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [http://www.ebi.ac.uk/pdbsum/3ffw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 3ffw" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3ffw" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Chemotaxis protein\|Chemotaxis protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:42, 8 February 2016

OCA — Mon, 08 Feb 2016 07:42:54 GMT

←Older revision		Revision as of 07:42, 8 February 2016
Line 2:		Line 2:
	<StructureSection load='3ffw' size='340' side='right' caption='[[3ffw]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3ffw' size='340' side='right' caption='[[3ffw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ffw]] is a 2 chain structure with 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=3FFW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FFW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ffw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FFW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <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=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <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">[[3f7n\|3f7n]], [[3fft\|3fft]], [[3ffx\|3ffx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3f7n\|3f7n]], [[3fft\|3fft]], [[3ffx\|3ffx]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1882, cheY, JW1871 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~562 Escherichia coli~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1882, cheY, JW1871 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [http://www.ebi.ac.uk/pdbsum/3ffw 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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [http://pdbe.org/3ffw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [http://www.ebi.ac.uk/pdbsum/3ffw PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=3ffw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 28:
	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 3ffw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Ecoli]]
	[[Category: Bourret, R B]]		[[Category: Bourret, R B]]
	[[Category: Collins, E J]]		[[Category: Collins, E J]]

OCA at 21:43, 24 December 2014

OCA — Wed, 24 Dec 2014 21:43:22 GMT

←Older revision		Revision as of 21:43, 24 December 2014
Line 8:		Line 8:
	<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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [http://www.ebi.ac.uk/pdbsum/3ffw 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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [http://www.ebi.ac.uk/pdbsum/3ffw PDBsum]</span></td></tr>
	</table>		</table>
		+	== 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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 14:14, 17 December 2014

OCA — Wed, 17 Dec 2014 14:14:11 GMT

←Older revision		Revision as of 14:14, 17 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3ffw\| PDB=3ffw \| SCENE= }}~~	+	==Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+==
-	===Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+===	+	<StructureSection load='3ffw' size='340' side='right' caption='[[3ffw]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19646451}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3ffw]] is a 2 chain structure with 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=3FFW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FFW FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <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">[[3f7n\|3f7n]], [[3fft\|3fft]], [[3ffx\|3ffx]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1882, cheY, JW1871 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3ffw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ffw RCSB], [http://www.ebi.ac.uk/pdbsum/3ffw PDBsum]</span></td></tr>
		+	</table>
		+	== 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/ff/3ffw_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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In two-component regulatory systems, covalent phosphorylation typically activates the response regulator signaling protein, and hydrolysis of the phosphoryl group reestablishes the inactive state. Despite highly conserved three-dimensional structures and active-site features, the rates of catalytic autodephosphorylation for different response regulators vary by a factor of almost 10(6). Previous studies identified two variable active-site residues, corresponding to Escherichia coli CheY residues 59 and 89, that modulate response regulator autodephosphorylation rates about 100-fold. Here, a set of five CheY mutants, which match other "model" response regulators (ArcA, CusR, DctD, FixJ, PhoB, or Spo0F) at variable active-site positions corresponding to CheY residues 14, 59, and 89, were characterized functionally and structurally in an attempt to identify mechanisms that modulate autodephosphorylation rate. As expected, the autodephosphorylation rates of the CheY mutants were reduced 6- to 40-fold relative to wild-type CheY, but all still autodephosphorylated 12- to 80-fold faster than their respective model response regulators. Comparison of X-ray crystal structures of the five CheY mutants (complexed with the phosphoryl group analogue BeF(3)(-)) to wild-type CheY or corresponding model response regulator structures gave strong evidence for steric obstruction of the phosphoryl group from the attacking water molecule as one mechanism to enhance phosphoryl group stability. Structural data also suggested that impeding the change of a response regulator from the active to the inactive conformation might retard the autodephosphorylation reaction if the two processes are coupled, and that the residue at position '58' may contribute to rate modulation. A given combination of amino acids at positions '14', '59', and '89' adopted similar conformations regardless of protein context (CheY or model response regulator), suggesting that knowledge of residue identity may be sufficient to predict autodephosphorylation rate, and hence the kinetics of the signaling response, in the response regulator family of proteins.

-	~~==About this Structure==~~	+	Matching biochemical reaction kinetics to the timescales of life: structural determinants that influence the autodephosphorylation rate of response regulator proteins.,Pazy Y, Wollish AC, Thomas SA, Miller PJ, Collins EJ, Bourret RB, Silversmith RE J Mol Biol. 2009 Oct 9;392(5):1205-20. Epub 2009 Jul 28. PMID:19646451<ref>PMID:19646451</ref>
-	~~[[3ffw]] is a 2 chain structure with 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=3FFW OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Chemotaxis protein\|Chemotaxis protein]]		*[[Chemotaxis protein\|Chemotaxis protein]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:019646451<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Bourret, R B.]]	+	[[Category: Bourret, R B]]
-	[[Category: Collins, E J.]]	+	[[Category: Collins, E J]]
-	[[Category: Pazy, Y.]]	+	[[Category: Pazy, Y]]
	[[Category: Bef3]]		[[Category: Bef3]]
	[[Category: Chemotaxis]]		[[Category: Chemotaxis]]

OCA at 10:57, 11 March 2013

OCA — Mon, 11 Mar 2013 10:57:43 GMT

←Older revision		Revision as of 10:57, 11 March 2013
Line 1:		Line 1:
-	[[Image:3ffw.png\|left\|200px]]
-
	{{STRUCTURE_3ffw\| PDB=3ffw \| SCENE= }}		{{STRUCTURE_3ffw\| PDB=3ffw \| SCENE= }}
-
	===Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+===		===Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+===
-
	{{ABSTRACT_PUBMED_19646451}}		{{ABSTRACT_PUBMED_19646451}}

OCA: Protected "3ffw" [edit=sysop:move=sysop]

OCA — Wed, 13 Feb 2013 11:19:20 GMT

Protected "3ffw" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:19, 13 February 2013

OCA at 11:19, 13 February 2013

OCA — Wed, 13 Feb 2013 11:19:14 GMT

←Older revision		Revision as of 11:19, 13 February 2013
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3ffw.png\|left\|200px]]
-	[[Image:3ffw.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3ffw", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3ffw\| PDB=3ffw \| SCENE= }}		{{STRUCTURE_3ffw\| PDB=3ffw \| SCENE= }}

	===Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+===		===Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19646451}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19646451 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19646451}}		{{ABSTRACT_PUBMED_19646451}}

	==About this Structure==		==About this Structure==
-	~~3FFW~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://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=3FFW OCA].	+	[[3ffw]] is a 2 chain structure with 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=3FFW OCA].
		+
		+	==See Also==
		+	*[[Chemotaxis protein\|Chemotaxis protein]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19646451~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019646451</ref><references group="xtra"/>
-	[[Category: Escherichia coli ~~k-12~~]]	+	[[Category: Escherichia coli]]
	[[Category: Bourret, R B.]]		[[Category: Bourret, R B.]]
	[[Category: Collins, E J.]]		[[Category: Collins, E J.]]
Line 30:		Line 21:
	[[Category: Bef3]]		[[Category: Bef3]]
	[[Category: Chemotaxis]]		[[Category: Chemotaxis]]
-	[[Category: Cytoplasm]]
	[[Category: Flagellar rotation]]		[[Category: Flagellar rotation]]
	[[Category: Magnesium]]		[[Category: Magnesium]]
Line 40:		Line 30:
	[[Category: Two-component regulatory system]]		[[Category: Two-component regulatory system]]
	[[Category: Two-component signal transduction]]		[[Category: Two-component signal transduction]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 23 08:48:16 2009''

OCA at 05:48, 23 September 2009

OCA — Wed, 23 Sep 2009 05:48:17 GMT

←Older revision		Revision as of 05:48, 23 September 2009
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3ffw.jpg\|left\|200px]]

-	The ~~entry 3ffw~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3ffw", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3ffw\| PDB=3ffw \| SCENE= }}

-	~~Authors: Pazy~~, Y., ~~Collins, E.J., Bourret, R.B.~~	+	===Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3- and Mn2+===

-	Description: Crystal Structure of CheY triple mutant F14Q, N59K, E89Y complexed with BeF3-and Mn2+

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jan 21 10~~:38:12 2009''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19646451}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19646451 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19646451}}
		+
		+	==About this Structure==
		+	3FFW is a 2 chains structure of sequences from [http://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=3FFW OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:19646451</ref><references group="xtra"/>
		+	[[Category: Escherichia coli k-12]]
		+	[[Category: Bourret, R B.]]
		+	[[Category: Collins, E J.]]
		+	[[Category: Pazy, Y.]]
		+	[[Category: Bef3]]
		+	[[Category: Chemotaxis]]
		+	[[Category: Cytoplasm]]
		+	[[Category: Flagellar rotation]]
		+	[[Category: Magnesium]]
		+	[[Category: Metal-binding]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: Receiver domain]]
		+	[[Category: Response regulator]]
		+	[[Category: Signaling protein]]
		+	[[Category: Two-component regulatory system]]
		+	[[Category: Two-component signal transduction]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 23 08:48:16 2009''