3rvm - Revision history

OCA at 12:38, 14 March 2024

2024-03-14T12:38:59Z

←Older revision		Revision as of 12:38, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3rvm' size='340' side='right'caption='[[3rvm]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='3rvm' size='340' side='right'caption='[[3rvm]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rvm]] is a 1 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=3RVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RVM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rvm]] 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=3RVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RVM FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 1.45Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'~~>~~[[1fqw\|1fqw]], [[3rvk\|3rvk]], [[3rvl\|3rvl]], [[3rvj\|3rvj]], [[3rvn\|3rvn]], [[3rvo\|3rvo]], [[3rvp\|3rvp]], [[3rvq\|3rvq]], [[3rvr\|3rvr]], [[3rvs\|3rvs]]~~<~~/div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=3rvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvm OCA], [https://pdbe.org/3rvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rvm RCSB], [https://www.ebi.ac.uk/pdbsum/3rvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rvm 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=3rvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvm OCA], [https://pdbe.org/3rvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rvm RCSB], [https://www.ebi.ac.uk/pdbsum/3rvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rvm 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>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Response regulator signaling proteins and phosphatases of the haloacid dehalogenase (HAD) superfamily share strikingly similar folds, active site geometries, and reaction chemistry. Proteins from both families catalyze the transfer of a phosphoryl group from a substrate to one of their own aspartyl residues, and subsequent hydrolysis of the phosphoprotein. Notable differences include an additional Asp that functions as an acid/base catalyst and an active site well-structured prior to phosphorylation in HAD phosphatases. Both features contribute to reactions substantially faster than those for response regulators. To investigate mechanisms underlying the functional differences between response regulators and HAD phosphatases, we characterized five double mutants of the response regulator CheY designed to mimic HAD phosphatases. Each mutant contained the extra Asp paired with a phosphatase-inspired substitution to potentially position the Asp properly. Only CheY DR (Arg as the anchor) exhibited enhanced rates of both autophosphorylation with phosphoramidate and autodephosphorylation compared to those of wild-type CheY. Crystal structures of CheY DR complexed with MoO4(2-) or WO4(2-) revealed active site hydrogen bonding networks similar to those in HAD.substrate complexes, with the extra Asp positioned for direct interaction with the leaving group (phosphorylation) or nucleophile (dephosphorylation). However, CheY DR reaction kinetics did not exhibit the pH sensitivities expected for acid/base catalysis. Biochemical analysis indicated CheY DR had an enhanced propensity to adopt the active conformation without phosphorylation, but a crystal structure revealed unphosphorylated CheY DR was not locked in the active conformation. Thus, the enhanced reactivity of CheY DR reflected partial acquisition of catalytic and structural features of HAD phosphatases.	+
-		+
-	Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases.,Immormino RM, Starbird CA, Silversmith RE, Bourret RB Biochemistry. 2015 Jun 9;54(22):3514-27. doi: 10.1021/acs.biochem.5b00286. Epub, 2015 May 28. PMID:25928369<ref>PMID:25928369</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3rvm" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 27:		Line 17:
	__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: Immormino~~, R M~~]]	+	[[Category: Immormino RM]]
-	[[Category: Silversmith~~, R E~~]]	+	[[Category: Silversmith RE]]
-	[[Category: Starbird~~, C A]]~~	+	[[Category: Starbird CA]]
-	~~[[Category: Beta-alpha protein]]~~	+
-	~~[[Category: Chea chex chez]]~~	+
-	~~[[Category: Chemotaxis]]~~	+
-	~~[[Category: Chey]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Response regulator]]~~	+
-	~~[[Category: Signal transduction]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Two-component~~]]	+

OCA at 10:27, 22 June 2022

2022-06-22T10:27:09Z

←Older revision		Revision as of 10:27, 22 June 2022
Line 1:		Line 1:

	==Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D and E89R==		==Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D and E89R==
-	<StructureSection load='3rvm' size='340' side='right' caption='[[3rvm]], [[Resolution\|resolution]] 1.45Å' scene=''>	+	<StructureSection load='3rvm' size='340' side='right'caption='[[3rvm]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rvm]] is a 1 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=3RVM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3RVM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rvm]] is a 1 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=3RVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RVM FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fqw\|1fqw]], [[3rvk\|3rvk]], [[3rvl\|3rvl]], [[3rvj\|3rvj]], [[3rvn\|3rvn]], [[3rvo\|3rvo]], [[3rvp\|3rvp]], [[3rvq\|3rvq]], [[3rvr\|3rvr]], [[3rvs\|3rvs]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fqw\|1fqw]], [[3rvk\|3rvk]], [[3rvl\|3rvl]], [[3rvj\|3rvj]], [[3rvn\|3rvn]], [[3rvo\|3rvo]], [[3rvp\|3rvp]], [[3rvq\|3rvq]], [[3rvr\|3rvr]], [[3rvs\|3rvs]]</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=3rvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvm OCA], [~~http~~://pdbe.org/3rvm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3rvm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3rvm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3rvm 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=3rvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvm OCA], [https://pdbe.org/3rvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rvm RCSB], [https://www.ebi.ac.uk/pdbsum/3rvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rvm 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:

	==See Also==		==See Also==
-	*[[Chemotaxis protein\|Chemotaxis protein]]	+	*[[Chemotaxis protein 3D structures\|Chemotaxis protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Ecoli]]		[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: Bourret, R B]]		[[Category: Bourret, R B]]
	[[Category: Immormino, R M]]		[[Category: Immormino, R M]]

OCA at 06:31, 21 September 2016

2016-09-21T06:31:42Z

←Older revision		Revision as of 06:31, 21 September 2016
Line 11:		Line 11:
	== 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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Response regulator signaling proteins and phosphatases of the haloacid dehalogenase (HAD) superfamily share strikingly similar folds, active site geometries, and reaction chemistry. Proteins from both families catalyze the transfer of a phosphoryl group from a substrate to one of their own aspartyl residues, and subsequent hydrolysis of the phosphoprotein. Notable differences include an additional Asp that functions as an acid/base catalyst and an active site well-structured prior to phosphorylation in HAD phosphatases. Both features contribute to reactions substantially faster than those for response regulators. To investigate mechanisms underlying the functional differences between response regulators and HAD phosphatases, we characterized five double mutants of the response regulator CheY designed to mimic HAD phosphatases. Each mutant contained the extra Asp paired with a phosphatase-inspired substitution to potentially position the Asp properly. Only CheY DR (Arg as the anchor) exhibited enhanced rates of both autophosphorylation with phosphoramidate and autodephosphorylation compared to those of wild-type CheY. Crystal structures of CheY DR complexed with MoO4(2-) or WO4(2-) revealed active site hydrogen bonding networks similar to those in HAD.substrate complexes, with the extra Asp positioned for direct interaction with the leaving group (phosphorylation) or nucleophile (dephosphorylation). However, CheY DR reaction kinetics did not exhibit the pH sensitivities expected for acid/base catalysis. Biochemical analysis indicated CheY DR had an enhanced propensity to adopt the active conformation without phosphorylation, but a crystal structure revealed unphosphorylated CheY DR was not locked in the active conformation. Thus, the enhanced reactivity of CheY DR reflected partial acquisition of catalytic and structural features of HAD phosphatases.
		+
		+	Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases.,Immormino RM, Starbird CA, Silversmith RE, Bourret RB Biochemistry. 2015 Jun 9;54(22):3514-27. doi: 10.1021/acs.biochem.5b00286. Epub, 2015 May 28. PMID:25928369<ref>PMID:25928369</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 3rvm" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 20:12, 4 August 2016

2016-08-04T20:12:46Z

←Older revision		Revision as of 20:12, 4 August 2016
Line 1:		Line 1:
		+
	==Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D and E89R==		==Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D and E89R==
	<StructureSection load='3rvm' size='340' side='right' caption='[[3rvm]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='3rvm' size='340' side='right' caption='[[3rvm]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rvm]] is a 1 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=3RVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RVM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rvm]] is a 1 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=3RVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RVM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fqw\|1fqw]], [[3rvk\|3rvk]], [[3rvl\|3rvl]], [[3rvj\|3rvj]], [[3rvn\|3rvn]], [[3rvo\|3rvo]], [[3rvp\|3rvp]], [[3rvq\|3rvq]], [[3rvr\|3rvr]], [[3rvs\|3rvs]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fqw\|1fqw]], [[3rvk\|3rvk]], [[3rvl\|3rvl]], [[3rvj\|3rvj]], [[3rvn\|3rvn]], [[3rvo\|3rvo]], [[3rvp\|3rvp]], [[3rvq\|3rvq]], [[3rvr\|3rvr]], [[3rvs\|3rvs]]</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=3rvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rvm RCSB], [http://www.ebi.ac.uk/pdbsum/3rvm 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=3rvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvm OCA], [http://pdbe.org/3rvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rvm RCSB], [http://www.ebi.ac.uk/pdbsum/3rvm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rvm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Ecoli]]
	[[Category: Bourret, R B]]		[[Category: Bourret, R B]]
	[[Category: Immormino, R M]]		[[Category: Immormino, R M]]

OCA at 12:44, 25 December 2014

2014-12-25T12:44:23Z

←Older revision		Revision as of 12:44, 25 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3rvm.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D and E89R==
		+	<StructureSection load='3rvm' size='340' side='right' caption='[[3rvm]], [[Resolution\|resolution]] 1.45Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3rvm]] is a 1 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=3RVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RVM FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fqw\|1fqw]], [[3rvk\|3rvk]], [[3rvl\|3rvl]], [[3rvj\|3rvj]], [[3rvn\|3rvn]], [[3rvo\|3rvo]], [[3rvp\|3rvp]], [[3rvq\|3rvq]], [[3rvr\|3rvr]], [[3rvs\|3rvs]]</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=3rvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rvm RCSB], [http://www.ebi.ac.uk/pdbsum/3rvm PDBsum]</span></td></tr>
		+	</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>

-	~~<!--~~	+	==See Also==
-	~~The line below this paragraph, containing "STRUCTURE_3rvm", creates the "Structure Box" on the page.~~	+	*[[Chemotaxis protein\|Chemotaxis protein]]
-	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~	+	== References ==
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+	<references/>
-	~~or leave the SCENE parameter empty for the default display.~~	+	__TOC__
-	~~-->~~	+	</StructureSection>
-	~~{{STRUCTURE_3rvm\| PDB~~=~~3rvm \| SCENE= }}~~	+
-		+
-	~~===Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D and E89R~~===	+
-		+
-		+
-	==~~About this Structure~~==	+
-	~~[[3rvm]] is a 1 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=3RVM OCA].~~	+
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Bourret, R B.]]	+	[[Category: Bourret, R B]]
-	[[Category: Immormino, R M.]]	+	[[Category: Immormino, R M]]
-	[[Category: Silversmith, R E.]]	+	[[Category: Silversmith, R E]]
-	[[Category: Starbird, C A.]]	+	[[Category: Starbird, C A]]
	[[Category: Beta-alpha protein]]		[[Category: Beta-alpha protein]]
	[[Category: Chea chex chez]]		[[Category: Chea chex chez]]

OCA at 09:20, 9 May 2012

2012-05-09T09:20:45Z

←Older revision		Revision as of 09:20, 9 May 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3rvm.jpg\|left\|200px]]

-	The ~~entry 3rvm~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3rvm", 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_3rvm\| PDB=3rvm \| SCENE= }}

-	~~Authors~~: ~~Starbird, C.A., Immormino, R.M., Silversmith, R.E., Bourret, R.B.~~	+	===Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D and E89R===

-	~~Description:~~ Structure ~~of the CheY-Mn2+ Complex~~ with ~~substitutions at 59 and 89~~: ~~N59D and E89R~~	+
		+	==About this Structure==
		+	[[3rvm]] is a 1 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=3RVM OCA].
		+	[[Category: Escherichia coli]]
		+	[[Category: Bourret, R B.]]
		+	[[Category: Immormino, R M.]]
		+	[[Category: Silversmith, R E.]]
		+	[[Category: Starbird, C A.]]
		+	[[Category: Beta-alpha protein]]
		+	[[Category: Chea chex chez]]
		+	[[Category: Chemotaxis]]
		+	[[Category: Chey]]
		+	[[Category: Phosphorylation]]
		+	[[Category: Response regulator]]
		+	[[Category: Signal transduction]]
		+	[[Category: Signaling protein]]
		+	[[Category: Two-component]]

OCA at 05:24, 1 June 2011

2011-06-01T05:24:08Z

←Older revision		Revision as of 05:24, 1 June 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3rvm is ON HOLD	+	The entry 3rvm is ON HOLD until Paper Publication

-	Authors: Starbird, C.A., Immormino, R.M., Silversmith, R.S., Bourret, R.B.	+	Authors: Starbird, C.A., Immormino, R.M., Silversmith, R.E., Bourret, R.B.

	Description: Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D and E89R		Description: Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D and E89R

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

2011-05-18T05:16:29Z

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

←Older revision

Revision as of 05:16, 18 May 2011

OCA: New page: '''Unreleased structure''' The entry 3rvm is ON HOLD Authors: Starbird, C.A., Immormino, R.M., Silversmith, R.S., Bourret, R.B. Description: Structure of the CheY-Mn2+ Complex with sub...

2011-05-18T05:16:28Z

New page: '''Unreleased structure''' The entry 3rvm is ON HOLD Authors: Starbird, C.A., Immormino, R.M., Silversmith, R.S., Bourret, R.B. Description: Structure of the CheY-Mn2+ Complex with sub...

New page

'''Unreleased structure'''

The entry 3rvm is ON HOLD

Authors: Starbird, C.A., Immormino, R.M., Silversmith, R.S., Bourret, R.B.

Description: Structure of the CheY-Mn2+ Complex with substitutions at 59 and 89: N59D and E89R