8dhy - Revision history

OCA at 10:09, 25 October 2023

2023-10-25T10:09:58Z

←Older revision		Revision as of 10:09, 25 October 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8dhy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DHY FirstGlance]. <br>		<table><tr><td colspan='2'>[[8dhy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DHY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]] 2.15Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=8dhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dhy OCA], [https://pdbe.org/8dhy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dhy RCSB], [https://www.ebi.ac.uk/pdbsum/8dhy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dhy ProSAT]</span></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=8dhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dhy OCA], [https://pdbe.org/8dhy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dhy RCSB], [https://www.ebi.ac.uk/pdbsum/8dhy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dhy ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:20, 7 December 2022

2022-12-07T08:20:35Z

←Older revision		Revision as of 08:20, 7 December 2022
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-	'''Unreleased structure'''

-	~~The entry~~ 8dhy is ~~ON HOLD until Paper~~ Publication	+	==N-terminal fragment of MsbA fused to GFP in complex with copper(II)==
		+	<StructureSection load='8dhy' size='340' side='right'caption='[[8dhy]], [[Resolution\|resolution]] 2.15Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8dhy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DHY FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=8dhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dhy OCA], [https://pdbe.org/8dhy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dhy RCSB], [https://www.ebi.ac.uk/pdbsum/8dhy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dhy ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/A0A059PIQ0_AEQVI A0A059PIQ0_AEQVI] [https://www.uniprot.org/uniprot/MSBA_ECOLI MSBA_ECOLI] Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	A critical step in lipopolysaccharide (LPS) biogenesis involves flipping lipooligosaccharide, an LPS precursor, from the cytoplasmic to the periplasmic leaflet of the inner membrane, an operation carried out by the ATP-binding cassette transporter MsbA. Although LPS binding to the inner cavity of MsbA is well established, the selectivity of MsbA-lipid interactions at other site(s) remains poorly understood. Here we use native mass spectrometry (MS) to characterize MsbA-lipid interactions and guide structural studies. We show the transporter co-purifies with copper(II) and metal binding modulates protein-lipid interactions. A 2.15 A resolution structure of an N-terminal region of MsbA in complex with copper(II) is presented, revealing a structure reminiscent of the GHK peptide, a high-affinity copper(II) chelator. Our results demonstrate conformation-dependent lipid binding affinities, particularly for the LPS-precursor, 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)(2)-lipid A (KDL). We report a 3.6 A-resolution structure of MsbA trapped in an open, outward-facing conformation with adenosine 5'-diphosphate and vanadate, revealing a distinct KDL binding site, wherein the lipid forms extensive interactions with the transporter. Additional studies provide evidence that the exterior KDL binding site is conserved and a positive allosteric modulator of ATPase activity, serving as a feedforward activation mechanism to couple transporter activity with LPS biosynthesis.

-	~~Authors~~:	+	Structural basis for lipid and copper regulation of the ABC transporter MsbA.,Lyu J, Liu C, Zhang T, Schrecke S, Elam NP, Packianathan C, Hochberg GKA, Russell D, Zhao M, Laganowsky A Nat Commun. 2022 Nov 26;13(1):7291. doi: 10.1038/s41467-022-34905-2. PMID:36435815<ref>PMID:36435815</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 8dhy" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Aequorea victoria]]
		+	[[Category: Escherichia coli]]
		+	[[Category: Large Structures]]
		+	[[Category: Laganowsky A]]
		+	[[Category: Lyu J]]
		+	[[Category: Schrecke SR]]
		+	[[Category: Zhang T]]

OCA at 03:53, 3 August 2022

2022-08-03T03:53:18Z

←Older revision		Revision as of 03:53, 3 August 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8dhy is ON HOLD	+	The entry 8dhy is ON HOLD until Paper Publication

	Authors:		Authors:

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

2022-07-06T15:14:21Z

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

←Older revision

Revision as of 15:14, 6 July 2022

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

2022-07-06T15:14:20Z

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

New page

'''Unreleased structure'''

The entry 8dhy is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]