4uey - Revision history

OCA at 08:21, 22 March 2023

OCA — Wed, 22 Mar 2023 08:21:05 GMT

←Older revision		Revision as of 08:21, 22 March 2023
Line 3:		Line 3:
	<StructureSection load='4uey' size='340' side='right'caption='[[4uey]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4uey' size='340' side='right'caption='[[4uey]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4uey]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4UEY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4uey]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UEY FirstGlance]. <br>
-	</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=4uey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uey OCA], [~~http~~://pdbe.org/4uey PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4uey RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4uey PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4uey ProSAT]</span></td></tr>	+	</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=4uey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uey OCA], [https://pdbe.org/4uey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uey RCSB], [https://www.ebi.ac.uk/pdbsum/4uey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uey ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PHOQ_SALTY PHOQ_SALTY]] Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.<ref>PMID:2544889</ref> <ref>PMID:9573193</ref> <ref>PMID:15910283</ref>	+	[https://www.uniprot.org/uniprot/PHOQ_SALTY PHOQ_SALTY] Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.<ref>PMID:2544889</ref> <ref>PMID:9573193</ref> <ref>PMID:15910283</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacillus cholerae-suis smith 1894]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hicks~~, K G~~]]	+	[[Category: Salmonella enterica]]
-	[[Category: Miller~~, S I~~]]	+	[[Category: Hicks KG]]
-	[[Category: Sancho-Vaello, E]]	+	[[Category: Miller SI]]
-	[[Category: Zeth, K]]	+	[[Category: Sancho-Vaello E]]
-	~~[[Category: Hamp domain]]~~	+	[[Category: Zeth K]]
-	~~[[Category: Histidine kinase]]~~	+
-	~~[[Category: Periplasmic domain]]~~	+
-	~~[[Category: Phoq]]~~	+
-	~~[[Category: Signal transduction]]~~	+
-	~~[[Category: Signaling protein~~]]	+

OCA at 11:12, 26 February 2020

OCA — Wed, 26 Feb 2020 11:12:13 GMT

←Older revision		Revision as of 11:12, 26 February 2020
Line 1:		Line 1:

	==Structure of the periplasmic domain PhoQ double mutant (W104C-A128C)==		==Structure of the periplasmic domain PhoQ double mutant (W104C-A128C)==
-	<StructureSection load='4uey' size='340' side='right' caption='[[4uey]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='4uey' size='340' side='right'caption='[[4uey]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4uey]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEY FirstGlance]. <br>		<table><tr><td colspan='2'>[[4uey]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEY FirstGlance]. <br>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Bacillus cholerae-suis smith 1894]]		[[Category: Bacillus cholerae-suis smith 1894]]
		+	[[Category: Large Structures]]
	[[Category: Hicks, K G]]		[[Category: Hicks, K G]]
	[[Category: Miller, S I]]		[[Category: Miller, S I]]

OCA at 06:24, 9 May 2018

OCA — Wed, 09 May 2018 06:24:15 GMT

←Older revision		Revision as of 06:24, 9 May 2018
Line 8:		Line 8:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PHOQ_SALTY PHOQ_SALTY]] Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.<ref>PMID:2544889</ref> <ref>PMID:9573193</ref> <ref>PMID:15910283</ref>		[[http://www.uniprot.org/uniprot/PHOQ_SALTY PHOQ_SALTY]] Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.<ref>PMID:2544889</ref> <ref>PMID:9573193</ref> <ref>PMID:15910283</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Salmonella PhoQ is a histidine kinase with a periplasmic sensor domain (PD) that promotes virulence by detecting the macrophage phagosome. PhoQ activity is repressed by divalent cations and induced in environments of acidic pH, limited divalent cations, and cationic antimicrobial peptides (CAMP). Previously, it was unclear which signals are sensed by salmonellae to promote PhoQ-mediated virulence. We defined conformational changes produced in the PhoQ PD on exposure to acidic pH that indicate structural flexibility is induced in alpha-helices 4 and 5, suggesting this region contributes to pH sensing. Therefore, we engineered a disulfide bond between W104C and A128C in the PhoQ PD that restrains conformational flexibility in alpha-helices 4 and 5. PhoQ(W104C-A128C) is responsive to CAMP, but is inhibited for activation by acidic pH and divalent cation limitation. phoQ(W104C-A128C) Salmonella enterica Typhimurium is virulent in mice, indicating that acidic pH and divalent cation sensing by PhoQ are dispensable for virulence.
		+
		+	Acidic pH and divalent cation sensing by PhoQ are dispensable for systemic salmonellae virulence.,Hicks KG, Delbecq SP, Sancho-Vaello E, Blanc MP, Dove KK, Prost LR, Daley ME, Zeth K, Klevit RE, Miller SI Elife. 2015 May 23;4:e06792. doi: 10.7554/eLife.06792. PMID:26002083<ref>PMID:26002083</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4uey" style="background-color:#fffaf0;"></div>

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

OCA at 05:45, 25 April 2018

OCA — Wed, 25 Apr 2018 05:45:11 GMT

←Older revision		Revision as of 05:45, 25 April 2018
Line 3:		Line 3:
	<StructureSection load='4uey' size='340' side='right' caption='[[4uey]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4uey' size='340' side='right' caption='[[4uey]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4uey]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4uey]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEY FirstGlance]. <br>
	</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=4uey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uey OCA], [http://pdbe.org/4uey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uey RCSB], [http://www.ebi.ac.uk/pdbsum/4uey PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uey ProSAT]</span></td></tr>		</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=4uey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uey OCA], [http://pdbe.org/4uey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uey RCSB], [http://www.ebi.ac.uk/pdbsum/4uey PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uey ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PHOQ_SALTY PHOQ_SALTY]] Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.<ref>PMID:2544889</ref> <ref>PMID:9573193</ref> <ref>PMID:15910283</ref>		[[http://www.uniprot.org/uniprot/PHOQ_SALTY PHOQ_SALTY]] Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.<ref>PMID:2544889</ref> <ref>PMID:9573193</ref> <ref>PMID:15910283</ref>
		+
		+	==See Also==
		+	*[[PhoP-PhoQ\|PhoP-PhoQ]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacillus cholerae-suis smith 1894]]
	[[Category: Hicks, K G]]		[[Category: Hicks, K G]]
	[[Category: Miller, S I]]		[[Category: Miller, S I]]

OCA at 14:24, 29 March 2017

OCA — Wed, 29 Mar 2017 14:24:29 GMT

←Older revision		Revision as of 14:24, 29 March 2017
Line 1:		Line 1:
		+
	==Structure of the periplasmic domain PhoQ double mutant (W104C-A128C)==		==Structure of the periplasmic domain PhoQ double mutant (W104C-A128C)==
	<StructureSection load='4uey' size='340' side='right' caption='[[4uey]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4uey' size='340' side='right' caption='[[4uey]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4uey]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEY FirstGlance]. <br>		<table><tr><td colspan='2'>[[4uey]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEY FirstGlance]. <br>
-	</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=4uey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uey OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uey RCSB], [http://www.ebi.ac.uk/pdbsum/4uey PDBsum]</span></td></tr>	+	</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=4uey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uey OCA], [http://pdbe.org/4uey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uey RCSB], [http://www.ebi.ac.uk/pdbsum/4uey PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uey ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 13:00, 24 June 2015

OCA — Wed, 24 Jun 2015 13:00:38 GMT

←Older revision		Revision as of 13:00, 24 June 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Structure of the periplasmic domain PhoQ double mutant (W104C-A128C)==
-		+	<StructureSection load='4uey' size='340' side='right' caption='[[4uey]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~The entry~~ 4uey is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4uey]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEY FirstGlance]. <br>
-	~~Authors~~: ~~Sancho~~-~~Vaello, E~~., ~~Hicks, K~~.G., ~~Miller, S~~.I., ~~Zeth, K~~.	+	</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=4uey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uey OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uey RCSB], [http://www.ebi.ac.uk/pdbsum/4uey PDBsum]</span></td></tr>
-		+	</table>
-	~~Description~~: ~~Structure~~ of the periplasmic ~~domain~~ PhoQ ~~double mutant~~ (~~W104C~~-~~A128C~~)	+	== Function ==
-	[[Category: ~~Unreleased Structures~~]]	+	[[http://www.uniprot.org/uniprot/PHOQ_SALTY PHOQ_SALTY]] Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.<ref>PMID:2544889</ref> <ref>PMID:9573193</ref> <ref>PMID:15910283</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Hicks, K G]]
		+	[[Category: Miller, S I]]
	[[Category: Sancho-Vaello, E]]		[[Category: Sancho-Vaello, E]]
-	[[Category: Hicks, K.G]]
-	[[Category: Miller, S.I]]
	[[Category: Zeth, K]]		[[Category: Zeth, K]]
		+	[[Category: Hamp domain]]
		+	[[Category: Histidine kinase]]
		+	[[Category: Periplasmic domain]]
		+	[[Category: Phoq]]
		+	[[Category: Signal transduction]]
		+	[[Category: Signaling protein]]

OCA: Protected "4uey" [edit=sysop:move=sysop]

OCA — Wed, 31 Dec 2014 12:45:33 GMT

Protected "4uey" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:45, 31 December 2014

OCA: New page: '''Unreleased structure''' The entry 4uey is ON HOLD Authors: Sancho-Vaello, E., Hicks, K.G., Miller, S.I., Zeth, K. Description: Structure of the periplasmic domain PhoQ double mutant...

OCA — Wed, 31 Dec 2014 12:45:31 GMT

New page: '''Unreleased structure''' The entry 4uey is ON HOLD Authors: Sancho-Vaello, E., Hicks, K.G., Miller, S.I., Zeth, K. Description: Structure of the periplasmic domain PhoQ double mutant...

New page

'''Unreleased structure'''

The entry 4uey is ON HOLD

Authors: Sancho-Vaello, E., Hicks, K.G., Miller, S.I., Zeth, K.

Description: Structure of the periplasmic domain PhoQ double mutant (W104C-A128C)
[[Category: Unreleased Structures]]
[[Category: Sancho-Vaello, E]]
[[Category: Hicks, K.G]]
[[Category: Miller, S.I]]
[[Category: Zeth, K]]