8alo - Revision history

OCA at 11:10, 14 March 2024

OCA — Thu, 14 Mar 2024 11:10:29 GMT

←Older revision		Revision as of 11:10, 14 March 2024
Line 9:		Line 9:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/TOXR_VIBCH TOXR_VIBCH] This transcription activator controls cholera toxin, pilus colonization factor and outer membrane protein expression in V.cholerae. It binds to the 5'-TTTTGAT-3' tandemly repeated DNA sequence in the cholera toxin promoter region. ToxS interacts with the C-terminal periplasmic domain of ToxR, stimulating its activity. It activates transcription at the promoters for tcpI and tcpA and this is presumably via ToxT.		[https://www.uniprot.org/uniprot/TOXR_VIBCH TOXR_VIBCH] This transcription activator controls cholera toxin, pilus colonization factor and outer membrane protein expression in V.cholerae. It binds to the 5'-TTTTGAT-3' tandemly repeated DNA sequence in the cholera toxin promoter region. ToxS interacts with the C-terminal periplasmic domain of ToxR, stimulating its activity. It activates transcription at the promoters for tcpI and tcpA and this is presumably via ToxT.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The seventh pandemic of the diarrheal cholera disease, which began in 1960, is caused by the Gram-negative bacterium Vibrio cholerae. Its environmental persistence provoking recurring sudden outbreaks is enabled by V. cholerae's rapid adaption to changing environments involving sensory proteins like ToxR and ToxS. Located at the inner membrane, ToxR and ToxS react to environmental stimuli like bile acid, thereby inducing survival strategies e.g. bile resistance and virulence regulation. The presented crystal structure of the sensory domains of ToxR and ToxS in combination with multiple bile acid interaction studies, reveals that a bile binding pocket of ToxS is only properly folded upon binding to ToxR. Our data proposes an interdependent functionality between ToxR transcriptional activity and ToxS sensory function. These findings support the previously suggested link between ToxRS and VtrAC-like co-component systems. Besides VtrAC, ToxRS is now the only experimentally determined structure within this recently defined superfamily, further emphasizing its significance. In-depth analysis of the ToxRS complex reveals its remarkable conservation across various Vibrio species, underlining the significance of conserved residues in the ToxS barrel and the more diverse ToxR sensory domain. Unravelling the intricate mechanisms governing ToxRS's environmental sensing capabilities, provides a promising tool for disruption of this vital interaction, ultimately inhibiting Vibrio's survival and virulence. Our findings hold far-reaching implications for all Vibrio strains that rely on the ToxRS system as a shared sensory cornerstone for adapting to their surroundings.

-	Vibrio cholerae's ToxRS bile sensing system.,Gubensak N, Sagmeister T, Buhlheller C, Geronimo BD, Wagner GE, Petrowitsch L, Grawert MA, Rotzinger M, Berger TMI, Schafer J, Uson I, Reidl J, Sanchez-Murcia PA, Zangger K, Pavkov-Keller T Elife. 2023 Sep 28;12:e88721. doi: 10.7554/eLife.88721. PMID:37768326<ref>PMID:37768326</ref>	+	==See Also==
-		+	*[[Transcriptional activator 3D structures\|Transcriptional activator 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 8alo" style="background-color:#fffaf0;"></div>~~	+
-	== ~~References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:26, 11 October 2023

OCA — Wed, 11 Oct 2023 08:26:32 GMT

←Older revision		Revision as of 08:26, 11 October 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8alo is ~~ON HOLD until 2025~~-02-01	+	==Heterodimer formation of sensory domains of Vibrio cholerae regulators ToxR and ToxS==
		+	<StructureSection load='8alo' size='340' side='right'caption='[[8alo]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8alo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ALO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ALO FirstGlance]. <br>
		+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3.002Å</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=8alo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8alo OCA], [https://pdbe.org/8alo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8alo RCSB], [https://www.ebi.ac.uk/pdbsum/8alo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8alo ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/TOXR_VIBCH TOXR_VIBCH] This transcription activator controls cholera toxin, pilus colonization factor and outer membrane protein expression in V.cholerae. It binds to the 5'-TTTTGAT-3' tandemly repeated DNA sequence in the cholera toxin promoter region. ToxS interacts with the C-terminal periplasmic domain of ToxR, stimulating its activity. It activates transcription at the promoters for tcpI and tcpA and this is presumably via ToxT.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The seventh pandemic of the diarrheal cholera disease, which began in 1960, is caused by the Gram-negative bacterium Vibrio cholerae. Its environmental persistence provoking recurring sudden outbreaks is enabled by V. cholerae's rapid adaption to changing environments involving sensory proteins like ToxR and ToxS. Located at the inner membrane, ToxR and ToxS react to environmental stimuli like bile acid, thereby inducing survival strategies e.g. bile resistance and virulence regulation. The presented crystal structure of the sensory domains of ToxR and ToxS in combination with multiple bile acid interaction studies, reveals that a bile binding pocket of ToxS is only properly folded upon binding to ToxR. Our data proposes an interdependent functionality between ToxR transcriptional activity and ToxS sensory function. These findings support the previously suggested link between ToxRS and VtrAC-like co-component systems. Besides VtrAC, ToxRS is now the only experimentally determined structure within this recently defined superfamily, further emphasizing its significance. In-depth analysis of the ToxRS complex reveals its remarkable conservation across various Vibrio species, underlining the significance of conserved residues in the ToxS barrel and the more diverse ToxR sensory domain. Unravelling the intricate mechanisms governing ToxRS's environmental sensing capabilities, provides a promising tool for disruption of this vital interaction, ultimately inhibiting Vibrio's survival and virulence. Our findings hold far-reaching implications for all Vibrio strains that rely on the ToxRS system as a shared sensory cornerstone for adapting to their surroundings.

-	~~Authors~~:	+	Vibrio cholerae's ToxRS bile sensing system.,Gubensak N, Sagmeister T, Buhlheller C, Geronimo BD, Wagner GE, Petrowitsch L, Grawert MA, Rotzinger M, Berger TMI, Schafer J, Uson I, Reidl J, Sanchez-Murcia PA, Zangger K, Pavkov-Keller T Elife. 2023 Sep 28;12:e88721. doi: 10.7554/eLife.88721. PMID:37768326<ref>PMID:37768326</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 8alo" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Vibrio cholerae]]
		+	[[Category: Bulheller C]]
		+	[[Category: Gubensaek N]]
		+	[[Category: Pavkov-Keller T]]
		+	[[Category: Sagmeister T]]
		+	[[Category: Wagner GE]]
		+	[[Category: Zangger K]]

OCA at 08:49, 2 August 2023

OCA — Wed, 02 Aug 2023 08:49:31 GMT

←Older revision		Revision as of 08:49, 2 August 2023
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8alo is ON HOLD until ~~2024~~-08-01	+	The entry 8alo is ON HOLD until 2025-02-01

	Authors:		Authors:

OCA at 15:22, 7 September 2022

OCA — Wed, 07 Sep 2022 15:22:40 GMT

←Older revision		Revision as of 15:22, 7 September 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8alo is ON HOLD	+	The entry 8alo is ON HOLD until 2024-08-01

	Authors:		Authors:

OCA: Protected "8alo" [edit=sysop:move=sysop]

OCA — Wed, 10 Aug 2022 03:56:33 GMT

Protected "8alo" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:56, 10 August 2022

OCA: New page: '''Unreleased structure''' The entry 8alo is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 10 Aug 2022 03:56:32 GMT

New page: '''Unreleased structure''' The entry 8alo is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8alo is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]