3m6m - Revision history

OCA at 08:31, 20 March 2024

2024-03-20T08:31:29Z

←Older revision		Revision as of 08:31, 20 March 2024
Line 1:		Line 1:

	==Crystal structure of RpfF complexed with REC domain of RpfC==		==Crystal structure of RpfF complexed with REC domain of RpfC==
-	<StructureSection load='3m6m' size='340' side='right' caption='[[3m6m]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='3m6m' size='340' side='right'caption='[[3m6m]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3m6m]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Xance Xance~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3M6M FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3m6m]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M6M FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.5Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Related_structure~~\|~~Related:]]</b></td><td class="sblockDat">[[3m6n\|3m6n~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~rpfF, XCC1857 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=340 XANCE])~~, ~~rpfC, XCC1856 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 XANCE])</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=3m6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6m OCA], [https://pdbe.org/3m6m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m6m RCSB], [https://www.ebi.ac.uk/pdbsum/3m6m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m6m ProSAT]</span></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3]~~ </~~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=3m6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6m OCA], [~~http~~://pdbe.org/3m6m PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3m6m RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3m6m PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3m6m ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~RPFC_XANCP RPFC_XANCP~~]] Member of the two-component regulatory system RpfG/RpfC, which is required for full virulence and for formation and dispersal of biofilms. Involved in sensing and responding to the diffusible signaling factor (DSF), which is essential for cell-cell signaling. RpfC is probably a sensor of environmental signals, including DSF, which is autophosphorylated at a histidine residue in response to the signal. Then, probably activates RpfG via a four-step phosphorelay. May also negatively regulate the production of DSF, independently of RpfG (By similarity).	+	[https://www.uniprot.org/uniprot/Q7CLS3_XANCP Q7CLS3_XANCP]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 22:		Line 20:
	</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=3m6m 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=3m6m ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The diffusible signal factor (DSF)-dependent quorum sensing (QS) system adopts a novel protein-protein interaction mechanism to autoregulate the production of signal DSF. Here, we present the crystal structures of DSF synthase RpfF and its complex with the REC domain of sensor protein RpfC. RpfF is structurally similarity to the members of the crotonase superfamily and contains an N-terminal alpha/beta spiral core domain and a C-terminal alpha-helical region. Further structural and mutational analysis identified two catalytic glutamate residues, which is the conserved feature of the enoyl-CoA hydratases/dehydratases. A putative substrate-binding pocket was unveiled and the key roles of the residues implicated in substrate binding were verified by mutational analysis. The binding of the REC domain may lock RpfF in an inactive conformation by blocking the entrance of substrate binding pocket, thereby negatively regulating DSF production. These findings provide a structural model for the RpfC-RpfF interaction-mediated QS autoinduction mechanism.
-
-	Structural basis of the sensor-synthase interaction in autoinduction of the quorum sensing signal DSF biosynthesis.,Cheng Z, He YW, Lim SC, Qamra R, Walsh MA, Zhang LH, Song H Structure. 2010 Sep 8;18(9):1199-209. PMID:20826346<ref>PMID:20826346</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3m6m" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Response regulator\|Response regulator]]	+	*[[Enoyl-CoA hydratase 3D structures\|Enoyl-CoA hydratase 3D structures]]
-	~~== References ==~~	+	*[[Response regulator 3D structure\|Response regulator 3D structure]]
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histidine kinase~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Xance~~]]	+	[[Category: Xanthomonas campestris pv. campestris]]
-	[[Category: Cheng, Z]]	+	[[Category: Cheng Z]]
-	[[Category: Lim~~, S C~~]]	+	[[Category: Lim SC]]
-	[[Category: Qamra, R]]	+	[[Category: Qamra R]]
-	[[Category: Song, H]]	+	[[Category: Song H]]
-	~~[[Category: Enoyl-coa hydratase]]~~	+
-	~~[[Category: Lyase-transferase complex]]~~	+
-	~~[[Category: Rec]]~~	+
-	~~[[Category: Rpfc]]~~	+
-	~~[[Category: Rpff~~]]	+

OCA at 06:55, 9 January 2019

2019-01-09T06:55:02Z

←Older revision		Revision as of 06:55, 9 January 2019
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m6/3m6m_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m6/3m6m_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>

OCA at 14:15, 5 August 2016

2016-08-05T14:15:52Z

←Older revision		Revision as of 14:15, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of RpfF complexed with REC domain of RpfC==		==Crystal structure of RpfF complexed with REC domain of RpfC==
	<StructureSection load='3m6m' size='340' side='right' caption='[[3m6m]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3m6m' size='340' side='right' caption='[[3m6m]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3m6m]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M6M FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3m6m]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Xance Xance]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M6M FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m6n\|3m6n]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m6n\|3m6n]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">rpfF, XCC1857 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 ~~Xanthomonas campestris pv. campestris~~]), rpfC, XCC1856 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 ~~Xanthomonas campestris pv. campestris~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">rpfF, XCC1857 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 XANCE]), rpfC, XCC1856 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 XANCE])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </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=3m6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m6m RCSB], [http://www.ebi.ac.uk/pdbsum/3m6m 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=3m6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6m OCA], [http://pdbe.org/3m6m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m6m RCSB], [http://www.ebi.ac.uk/pdbsum/3m6m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m6m ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	<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=3m6m ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	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 3m6m" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Histidine kinase]]		[[Category: Histidine kinase]]
-	[[Category: ~~Xanthomonas campestris pv. campestris~~]]	+	[[Category: Xance]]
	[[Category: Cheng, Z]]		[[Category: Cheng, Z]]
	[[Category: Lim, S C]]		[[Category: Lim, S C]]

OCA at 03:11, 25 December 2014

2014-12-25T03:11:07Z

←Older revision		Revision as of 03:11, 25 December 2014
Line 9:		Line 9:
	<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=3m6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m6m RCSB], [http://www.ebi.ac.uk/pdbsum/3m6m 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=3m6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m6m RCSB], [http://www.ebi.ac.uk/pdbsum/3m6m PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RPFC_XANCP RPFC_XANCP]] Member of the two-component regulatory system RpfG/RpfC, which is required for full virulence and for formation and dispersal of biofilms. Involved in sensing and responding to the diffusible signaling factor (DSF), which is essential for cell-cell signaling. RpfC is probably a sensor of environmental signals, including DSF, which is autophosphorylated at a histidine residue in response to the signal. Then, probably activates RpfG via a four-step phosphorelay. May also negatively regulate the production of DSF, independently of RpfG (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 15:45, 18 December 2014

2014-12-18T15:45:26Z

←Older revision		Revision as of 15:45, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3m6m~~\| ~~PDB~~=3m6m \| ~~SCENE~~= }}	+	==Crystal structure of RpfF complexed with REC domain of RpfC==
-	===~~Crystal~~ structure of RpfF ~~complexed~~ with REC domain of RpfC~~===~~	+	<StructureSection load='3m6m' size='340' side='right' caption='[[3m6m]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20826346}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3m6m]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M6M FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m6n\|3m6n]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">rpfF, XCC1857 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 Xanthomonas campestris pv. campestris]), rpfC, XCC1856 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 Xanthomonas campestris pv. campestris])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </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=3m6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m6m RCSB], [http://www.ebi.ac.uk/pdbsum/3m6m 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/m6/3m6m_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 ==
		+	The diffusible signal factor (DSF)-dependent quorum sensing (QS) system adopts a novel protein-protein interaction mechanism to autoregulate the production of signal DSF. Here, we present the crystal structures of DSF synthase RpfF and its complex with the REC domain of sensor protein RpfC. RpfF is structurally similarity to the members of the crotonase superfamily and contains an N-terminal alpha/beta spiral core domain and a C-terminal alpha-helical region. Further structural and mutational analysis identified two catalytic glutamate residues, which is the conserved feature of the enoyl-CoA hydratases/dehydratases. A putative substrate-binding pocket was unveiled and the key roles of the residues implicated in substrate binding were verified by mutational analysis. The binding of the REC domain may lock RpfF in an inactive conformation by blocking the entrance of substrate binding pocket, thereby negatively regulating DSF production. These findings provide a structural model for the RpfC-RpfF interaction-mediated QS autoinduction mechanism.

-	~~==Function==~~	+	Structural basis of the sensor-synthase interaction in autoinduction of the quorum sensing signal DSF biosynthesis.,Cheng Z, He YW, Lim SC, Qamra R, Walsh MA, Zhang LH, Song H Structure. 2010 Sep 8;18(9):1199-209. PMID:20826346<ref>PMID:20826346</ref>
-	~~[[http://www.uniprot.org/uniprot/RPFC_XANCP RPFC_XANCP]] Member~~ of the ~~two~~-~~component regulatory system RpfG/RpfC, which is required for full virulence and for formation and dispersal~~ of ~~biofilms. Involved in~~ sensing ~~and responding to the diffusible signaling factor (~~DSF~~), which is essential for cell-cell signaling~~. ~~RpfC is probably a sensor of environmental signals~~, ~~including DSF~~, ~~which is autophosphorylated at a histidine residue in response to the signal. Then~~, ~~probably activates RpfG via a four-step phosphorelay~~. ~~May also negatively regulate the production of DSF, independently of RpfG~~ (~~By similarity~~).	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3m6m]] is~~ a ~~6 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Xanthomonas_campestris_pv~~.~~_campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Response regulator\|Response regulator]]		*[[Response regulator\|Response regulator]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020826346</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Histidine kinase]]		[[Category: Histidine kinase]]
	[[Category: Xanthomonas campestris pv. campestris]]		[[Category: Xanthomonas campestris pv. campestris]]
-	[[Category: Cheng, Z.]]	+	[[Category: Cheng, Z]]
-	[[Category: Lim, S C.]]	+	[[Category: Lim, S C]]
-	[[Category: Qamra, R.]]	+	[[Category: Qamra, R]]
-	[[Category: Song, H.]]	+	[[Category: Song, H]]
	[[Category: Enoyl-coa hydratase]]		[[Category: Enoyl-coa hydratase]]
	[[Category: Lyase-transferase complex]]		[[Category: Lyase-transferase complex]]

OCA at 06:42, 16 October 2013

2013-10-16T06:42:42Z

←Older revision		Revision as of 06:42, 16 October 2013
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-	[[Image:3m6m.png\|left\|200px]]
-
	{{STRUCTURE_3m6m\| PDB=3m6m \| SCENE= }}		{{STRUCTURE_3m6m\| PDB=3m6m \| SCENE= }}
-
	===Crystal structure of RpfF complexed with REC domain of RpfC===		===Crystal structure of RpfF complexed with REC domain of RpfC===
		+	{{ABSTRACT_PUBMED_20826346}}

-	~~{{ABSTRACT_PUBMED_20826346}}~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/RPFC_XANCP RPFC_XANCP]] Member of the two-component regulatory system RpfG/RpfC, which is required for full virulence and for formation and dispersal of biofilms. Involved in sensing and responding to the diffusible signaling factor (DSF), which is essential for cell-cell signaling. RpfC is probably a sensor of environmental signals, including DSF, which is autophosphorylated at a histidine residue in response to the signal. Then, probably activates RpfG via a four-step phosphorelay. May also negatively regulate the production of DSF, independently of RpfG (By similarity).

	==About this Structure==		==About this Structure==
Line 14:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020826346</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020826346</ref><references group="xtra"/><references/>
	[[Category: Histidine kinase]]		[[Category: Histidine kinase]]
	[[Category: Xanthomonas campestris pv. campestris]]		[[Category: Xanthomonas campestris pv. campestris]]

OCA at 11:59, 20 October 2012

2012-10-20T11:59:24Z

←Older revision		Revision as of 11:59, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3m6m]] is a 6 chain structure ~~of [[Response regulator]]~~ with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA].	+	[[3m6m]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA].

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

OCA: Protected "3m6m" [edit=sysop:move=sysop]

2012-07-26T07:15:51Z

Protected "3m6m" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:15, 26 July 2012

OCA at 07:15, 26 July 2012

2012-07-26T07:15:49Z

←Older revision		Revision as of 07:15, 26 July 2012
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3m6m.png\|left\|200px]]
-	[[Image:3m6m.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3m6m", 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_3m6m\| PDB=3m6m \| SCENE= }}		{{STRUCTURE_3m6m\| PDB=3m6m \| SCENE= }}

	===Crystal structure of RpfF complexed with REC domain of RpfC===		===Crystal structure of RpfF complexed with REC domain of RpfC===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20826346}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20826346 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20826346}}		{{ABSTRACT_PUBMED_20826346}}

	==About this Structure==		==About this Structure==
-	~~3M6M~~ is a 6 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA].	+	[[3m6m]] is a 6 chain structure of [[Response regulator]] with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA].
		+
		+	==See Also==
		+	*[[Response regulator\|Response regulator]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20826346~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020826346</ref><references group="xtra"/>
	[[Category: Histidine kinase]]		[[Category: Histidine kinase]]
	[[Category: Xanthomonas campestris pv. campestris]]		[[Category: Xanthomonas campestris pv. campestris]]
Line 35:		Line 26:
	[[Category: Rpfc]]		[[Category: Rpfc]]
	[[Category: Rpff]]		[[Category: Rpff]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 14:46:23 2010''

OCA at 11:37, 22 September 2010

2010-09-22T11:37:25Z

←Older revision		Revision as of 11:37, 22 September 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3m6m.jpg\|left\|200px]]

-	The ~~entry 3m6m~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3m6m", 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_3m6m\| PDB=3m6m \| SCENE= }}

-	~~Authors: Cheng, Z., Lim, S.C., Qamra, R., Song, H.~~	+	===Crystal structure of RpfF complexed with REC domain of RpfC===

-	Description: Crystal structure of RpfF complexed with REC domain of RpfC

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Jun 10 10~~:57:10 2010''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20826346}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20826346 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20826346}}
		+
		+	==About this Structure==
		+	3M6M is a 6 chains structure with sequences from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6M OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20826346</ref><references group="xtra"/>
		+	[[Category: Histidine kinase]]
		+	[[Category: Xanthomonas campestris pv. campestris]]
		+	[[Category: Cheng, Z.]]
		+	[[Category: Lim, S C.]]
		+	[[Category: Qamra, R.]]
		+	[[Category: Song, H.]]
		+	[[Category: Enoyl-coa hydratase]]
		+	[[Category: Lyase-transferase complex]]
		+	[[Category: Rec]]
		+	[[Category: Rpfc]]
		+	[[Category: Rpff]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 14:46:23 2010''