8pek - Revision history

OCA at 08:02, 1 May 2024

OCA — Wed, 01 May 2024 08:02:44 GMT

←Older revision		Revision as of 08:02, 1 May 2024
Line 9:		Line 9:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/V5YUQ0_SERMA V5YUQ0_SERMA] Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.[ARBA:ARBA00003540]		[https://www.uniprot.org/uniprot/V5YUQ0_SERMA V5YUQ0_SERMA] Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.[ARBA:ARBA00003540]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Active nutrient uptake is fundamental for survival and pathogenicity of Gram-negative bacteria, which operate a multi-protein Ton system to transport essential nutrients like metals and vitamins. This system harnesses the proton motive force at the inner membrane to energize the import through the outer membrane, but the mechanism of energy transfer remains enigmatic. Here, we study the periplasmic domain of ExbD, a crucial component of the proton channel of the Ton system. We show that this domain is a dynamic dimer switching between two conformations representing the proton channel's open and closed states. By in vivo phenotypic assays we demonstrate that this conformational switch is essential for the nutrient uptake by bacteria. The open state of ExbD triggers a disorder to order transition of TonB, enabling TonB to supply energy to the nutrient transporter. We also reveal the anchoring role of the peptidoglycan layer in this mechanism. Herein, we propose a mechanistic model for the Ton system, emphasizing ExbD duality and the pivotal catalytic role of peptidoglycan. Sequence analysis suggests that this mechanism is conserved in other systems energizing gliding motility and membrane integrity. Our study fills important gaps in understanding bacterial motor mechanism and proposes novel antibacterial strategies.
-
-	Ton Motor Conformational Switch and Peptidoglycan Role in Bacterial Nutrient Uptake.,Zinke M, Lejeune M, Mechaly A, Bardiaux B, Boneca IG, Delepelaire P, Izadi-Pruneyre N bioRxiv. 2023 Aug 11:2023.08.11.552980. doi: 10.1101/2023.08.11.552980. Preprint. PMID:37609138<ref>PMID:37609138</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 8pek" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:27, 6 September 2023

OCA — Wed, 06 Sep 2023 06:27:00 GMT

←Older revision		Revision as of 06:27, 6 September 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8pek is ~~ON HOLD until Paper~~ Publication	+	==Structure of the dimeric, periplasmic domain of ExbD==
		+	<StructureSection load='8pek' size='340' side='right'caption='[[8pek]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8pek]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8PEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PEK FirstGlance]. <br>
		+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=8pek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8pek OCA], [https://pdbe.org/8pek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8pek RCSB], [https://www.ebi.ac.uk/pdbsum/8pek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8pek ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/V5YUQ0_SERMA V5YUQ0_SERMA] Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.[ARBA:ARBA00003540]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Active nutrient uptake is fundamental for survival and pathogenicity of Gram-negative bacteria, which operate a multi-protein Ton system to transport essential nutrients like metals and vitamins. This system harnesses the proton motive force at the inner membrane to energize the import through the outer membrane, but the mechanism of energy transfer remains enigmatic. Here, we study the periplasmic domain of ExbD, a crucial component of the proton channel of the Ton system. We show that this domain is a dynamic dimer switching between two conformations representing the proton channel's open and closed states. By in vivo phenotypic assays we demonstrate that this conformational switch is essential for the nutrient uptake by bacteria. The open state of ExbD triggers a disorder to order transition of TonB, enabling TonB to supply energy to the nutrient transporter. We also reveal the anchoring role of the peptidoglycan layer in this mechanism. Herein, we propose a mechanistic model for the Ton system, emphasizing ExbD duality and the pivotal catalytic role of peptidoglycan. Sequence analysis suggests that this mechanism is conserved in other systems energizing gliding motility and membrane integrity. Our study fills important gaps in understanding bacterial motor mechanism and proposes novel antibacterial strategies.

-	~~Authors~~:	+	Ton Motor Conformational Switch and Peptidoglycan Role in Bacterial Nutrient Uptake.,Zinke M, Lejeune M, Mechaly A, Bardiaux B, Boneca IG, Delepelaire P, Izadi-Pruneyre N bioRxiv. 2023 Aug 11:2023.08.11.552980. doi: 10.1101/2023.08.11.552980. Preprint. PMID:37609138<ref>PMID:37609138</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 8pek" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Serratia marcescens]]
		+	[[Category: Bardiaux B]]
		+	[[Category: Izadi-Pruneyre N]]
		+	[[Category: Zinke M]]

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

OCA — Wed, 21 Jun 2023 08:25:52 GMT

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

←Older revision

Revision as of 08:25, 21 June 2023

OCA: New page: '''Unreleased structure''' The entry 8pek is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

OCA — Wed, 21 Jun 2023 08:25:51 GMT

New page: '''Unreleased structure''' The entry 8pek is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8pek is ON HOLD until Paper Publication

Authors:

Description:
[[Category: Unreleased Structures]]