6v8q - Revision history

OCA at 14:36, 6 March 2024

OCA — Wed, 06 Mar 2024 14:36:28 GMT

←Older revision		Revision as of 14:36, 6 March 2024
Line 3:		Line 3:
	<StructureSection load='6v8q' size='340' side='right'caption='[[6v8q]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='6v8q' size='340' side='right'caption='[[6v8q]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6v8q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V8Q OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca.weizmann~~.~~ac.il/oca-docs~~/fgij/fg.htm?mol=6V8Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6v8q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._14028S Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V8Q FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=QSR:(9Z,21R,24R,30R,33R,44Z)-24,27,30-trihydroxy-18,24,30,36-tetraoxo-19,23,25,29,31,35-hexaoxa-24lambda~5~,30lambda~5~-~~diphosphatripentaconta~~-9,44-diene-21,33-diyl+(9Z,9Z)di-octadec-9-enoate'>QSR</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]] 2.699585Å</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=6v8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v8q OCA], [~~http~~://pdbe.org/6v8q PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6v8q RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6v8q PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6v8q ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=QSR:(9Z,21R,24R,30R,33R,44Z)-24,27,30-trihydroxy-18,24,30,36-tetraoxo-19,23,25,29,31,35-hexaoxa-24lambda~5~,30lambda~5~-dip+hosphatripentaconta-9,44-diene-21,33-diyl+(9Z,9Z)di-octadec-9-enoate'>QSR</scene></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=6v8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v8q OCA], [https://pdbe.org/6v8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v8q RCSB], [https://www.ebi.ac.uk/pdbsum/6v8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v8q ProSAT]</span></td></tr>
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/YEJM_SALTY YEJM_SALTY]
-	The Salmonella enterica subsp. enterica serovar Typhimurium PhoPQ two-component system is activated within the intracellular phagosome environment, where it promotes remodeling of the outer membrane and resistance to innate immune antimicrobial peptides. Maintenance of the PhoPQ-regulated outer membrane barrier requires PbgA, an inner membrane protein with a transmembrane domain essential for growth, and a periplasmic domain required for PhoPQ-activated increases in outer membrane cardiolipin. Here, we report the crystal structure of cardiolipin-bound PbgA, adopting a novel transmembrane fold that features a cardiolipin binding site in close proximity to a long and deep cleft spanning the lipid bilayer. The end of the cleft extends into the periplasmic domain of the protein, which is structurally coupled to the transmembrane domain via a functionally critical C-terminal helix. In conjunction with a conserved putative catalytic dyad situated at the middle of the cleft, our structural and mutational analyses suggest that PbgA is a multifunction membrane protein that mediates cardiolipin transport, a function essential for growth, and perhaps catalysis of an unknown enzymatic reaction.IMPORTANCE Gram-negative bacteria cause many types of infections and have become increasingly resistant to available antibiotic drugs. The outer membrane serves as an important barrier that protects bacteria against antibiotics and other toxic compounds. This outer membrane barrier function is regulated when bacteria are in host environments, and the protein PbgA contributes significantly to this increased barrier function by transporting cardiolipin to the outer membrane. We determined the crystal structure of PbgA in complex with cardiolipin and propose a model for its function. Knowledge of the mechanisms of outer membrane assembly and integrity can greatly contribute to the development of new and effective antibiotics, and this structural information may be useful in this regard.	+
-		+
-	~~Structure of an Inner Membrane Protein Required for PhoPQ-Regulated Increases in Outer Membrane Cardiolipin.,Fan J, Petersen EM, Hinds TR, Zheng N, Miller SI mBio. 2020 Feb 11;11(1). pii~~: ~~mBio.03277-19. doi: 10.1128~~/~~mBio.03277-19. PMID:32047135<ref>PMID:32047135<~~/~~ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 6v8q" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references~~/>	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Fan, J~~]]	+	[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S]]
-	[[Category: ~~Miller, S~~]]	+	[[Category: Fan J]]
-	[[Category: ~~Cl transport]]~~	+	[[Category: Miller S]]
-	~~[[Category: Membrane protein]]~~	+
-	~~[[Category: Outer membrane barrier]]~~	+
-	~~[[Category: Pbga]]~~	+
-	~~[[Category: Phopq~~]]	+

OCA at 09:59, 18 March 2020

OCA — Wed, 18 Mar 2020 09:59:50 GMT

←Older revision		Revision as of 09:59, 18 March 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6v8q is ~~ON HOLD until Paper~~ Publication	+	==Structure of an inner membrane protein required for PhoPQ regulated increases in outer membrane cardiolipin==
		+	<StructureSection load='6v8q' size='340' side='right'caption='[[6v8q]], [[Resolution\|resolution]] 2.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6v8q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V8Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6V8Q FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=QSR:(9Z,21R,24R,30R,33R,44Z)-24,27,30-trihydroxy-18,24,30,36-tetraoxo-19,23,25,29,31,35-hexaoxa-24lambda~5~,30lambda~5~-diphosphatripentaconta-9,44-diene-21,33-diyl+(9Z,9Z)di-octadec-9-enoate'>QSR</scene></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=6v8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v8q OCA], [http://pdbe.org/6v8q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v8q RCSB], [http://www.ebi.ac.uk/pdbsum/6v8q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v8q ProSAT]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The Salmonella enterica subsp. enterica serovar Typhimurium PhoPQ two-component system is activated within the intracellular phagosome environment, where it promotes remodeling of the outer membrane and resistance to innate immune antimicrobial peptides. Maintenance of the PhoPQ-regulated outer membrane barrier requires PbgA, an inner membrane protein with a transmembrane domain essential for growth, and a periplasmic domain required for PhoPQ-activated increases in outer membrane cardiolipin. Here, we report the crystal structure of cardiolipin-bound PbgA, adopting a novel transmembrane fold that features a cardiolipin binding site in close proximity to a long and deep cleft spanning the lipid bilayer. The end of the cleft extends into the periplasmic domain of the protein, which is structurally coupled to the transmembrane domain via a functionally critical C-terminal helix. In conjunction with a conserved putative catalytic dyad situated at the middle of the cleft, our structural and mutational analyses suggest that PbgA is a multifunction membrane protein that mediates cardiolipin transport, a function essential for growth, and perhaps catalysis of an unknown enzymatic reaction.IMPORTANCE Gram-negative bacteria cause many types of infections and have become increasingly resistant to available antibiotic drugs. The outer membrane serves as an important barrier that protects bacteria against antibiotics and other toxic compounds. This outer membrane barrier function is regulated when bacteria are in host environments, and the protein PbgA contributes significantly to this increased barrier function by transporting cardiolipin to the outer membrane. We determined the crystal structure of PbgA in complex with cardiolipin and propose a model for its function. Knowledge of the mechanisms of outer membrane assembly and integrity can greatly contribute to the development of new and effective antibiotics, and this structural information may be useful in this regard.

-	~~Authors~~:	+	Structure of an Inner Membrane Protein Required for PhoPQ-Regulated Increases in Outer Membrane Cardiolipin.,Fan J, Petersen EM, Hinds TR, Zheng N, Miller SI mBio. 2020 Feb 11;11(1). pii: mBio.03277-19. doi: 10.1128/mBio.03277-19. PMID:32047135<ref>PMID:32047135</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6v8q" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Fan, J]]
		+	[[Category: Miller, S]]
		+	[[Category: Cl transport]]
		+	[[Category: Membrane protein]]
		+	[[Category: Outer membrane barrier]]
		+	[[Category: Pbga]]
		+	[[Category: Phopq]]

OCA at 06:47, 1 January 2020

OCA — Wed, 01 Jan 2020 06:47:35 GMT

←Older revision		Revision as of 06:47, 1 January 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6v8q is ON HOLD	+	The entry 6v8q is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6v8q" [edit=sysop:move=sysop]

OCA — Wed, 18 Dec 2019 06:07:36 GMT

Protected "6v8q" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:07, 18 December 2019

OCA: New page: '''Unreleased structure''' The entry 6v8q is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 18 Dec 2019 06:07:35 GMT

New page: '''Unreleased structure''' The entry 6v8q is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6v8q is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]