6bug - Revision history

OCA at 11:04, 30 October 2024

2024-10-30T11:04:03Z

← Older revision		Revision as of 11:04, 30 October 2024
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	==Crystal structure of a membrane protein, crystal form I==		==Crystal structure of a membrane protein, crystal form I==
	<StructureSection load='6bug' size='340' side='right' caption='[[6bug]], [[Resolution\|resolution]] 3.27Å' scene=''>		<StructureSection load='6bug' size='340' side='right'caption='[[6bug]], [[Resolution\|resolution]] 3.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6bug]] is a 7 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_19258 Atcc 19258~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BUG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6BUG FirstGlance]. <br>		<table><tr><td colspan='2'>[[6bug]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_thermophilus Streptococcus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BUG FirstGlance]. <br>
	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=SEP:PHOSPHOSERINE'>SEP</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]] 3.27Å</td></tr>
	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~dltC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=1308 ATCC 19258]), dltB ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1308 ATCC 19258])~~</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=6bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bug OCA], [~~http~~://pdbe.org/6bug PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6bug RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6bug PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6bug 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=6bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bug OCA], [https://pdbe.org/6bug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bug RCSB], [https://www.ebi.ac.uk/pdbsum/6bug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bug ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/~~DLTC_STRT1 DLTC_STRT1]~~] Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.		[https://www.uniprot.org/uniprot/DLTC_STRT2 DLTC_STRT2] Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.[HAMAP-Rule:MF_00565]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Atcc 19258~~]]		[[Category: Large Structures]]
	[[Category: ~~Ma, D~~]]		[[Category: Streptococcus thermophilus]]
	[[Category: ~~Wang, Z~~]]		[[Category: Ma D]]
	[[Category: ~~Xu, W~~]]		[[Category: Wang Z]]
	[[Category: ~~Membrane protein~~]]		[[Category: Xu W]]

OCA at 08:33, 17 October 2018

2018-10-17T08:33:22Z

← Older revision		Revision as of 08:33, 17 October 2018
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	<StructureSection load='6bug' size='340' side='right' caption='[[6bug]], [[Resolution\|resolution]] 3.27Å' scene=''>		<StructureSection load='6bug' size='340' side='right' caption='[[6bug]], [[Resolution\|resolution]] 3.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6bug]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BUG FirstGlance]. <br>		<table><tr><td colspan='2'>[[6bug]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19258 Atcc 19258]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BUG FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dltC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1308 ATCC 19258]), dltB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1308 ATCC 19258])</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=6bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bug OCA], [http://pdbe.org/6bug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bug RCSB], [http://www.ebi.ac.uk/pdbsum/6bug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bug ProSAT]</span></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=6bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bug OCA], [http://pdbe.org/6bug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bug RCSB], [http://www.ebi.ac.uk/pdbsum/6bug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bug ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/DLTC_STRT1 DLTC_STRT1]] Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.		[[http://www.uniprot.org/uniprot/DLTC_STRT1 DLTC_STRT1]] Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Membrane-bound O-acyltransferases (MBOATs) are a superfamily of integral transmembrane enzymes that are found in all kingdoms of life(1). In bacteria, MBOATs modify protective cell-surface polymers. In vertebrates, some MBOAT enzymes-such as acyl-coenzyme A:cholesterol acyltransferase and diacylglycerol acyltransferase 1-are responsible for lipid biosynthesis or phospholipid remodelling(2,3). Other MBOATs, including porcupine, hedgehog acyltransferase and ghrelin acyltransferase, catalyse essential lipid modifications of secreted proteins such as Wnt, hedgehog and ghrelin, respectively(4-10). Although many MBOAT proteins are important drug targets, little is known about their molecular architecture and functional mechanisms. Here we present crystal structures of DltB, an MBOAT responsible for the D-alanylation of cell-wall teichoic acid in Gram-positive bacteria(11-16), both alone and in complex with the D-alanyl donor protein DltC. DltB contains a ring of 11 peripheral transmembrane helices, which shield a highly conserved extracellular structural funnel extending into the middle of the lipid bilayer. The conserved catalytic histidine residue is located at the bottom of this funnel and is connected to the intracellular DltC through a narrow tunnel. Mutation of either the catalytic histidine or the DltC-binding site of DltB abolishes the D-alanylation of lipoteichoic acid and sensitizes the Gram-positive bacterium Bacillus subtilis to cell-wall stress, which suggests cross-membrane catalysis involving the tunnel. Structure-guided sequence comparison among DltB and vertebrate MBOATs reveals a conserved structural core and suggests that MBOATs from different organisms have similar catalytic mechanisms. Our structures provide a template for understanding structure-function relationships in MBOATs and for developing therapeutic MBOAT inhibitors.

			Crystal structure of a membrane-bound O-acyltransferase.,Ma D, Wang Z, Merrikh CN, Lang KS, Lu P, Li X, Merrikh H, Rao Z, Xu W Nature. 2018 Oct;562(7726):286-290. doi: 10.1038/s41586-018-0568-2. Epub 2018 Oct, 3. PMID:30283133<ref>PMID:30283133</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 6bug" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Atcc 19258]]
	[[Category: Ma, D]]		[[Category: Ma, D]]
	[[Category: Wang, Z]]		[[Category: Wang, Z]]
	[[Category: Xu, W]]		[[Category: Xu, W]]
	[[Category: Membrane protein]]		[[Category: Membrane protein]]

OCA at 08:04, 10 October 2018

2018-10-10T08:04:50Z

← Older revision		Revision as of 08:04, 10 October 2018
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	~~'''Unreleased structure'''~~

	The ~~entry 6bug~~ is ~~ON HOLD until Paper Publication~~		==Crystal structure of a membrane protein, crystal form I==
			<StructureSection load='6bug' size='340' side='right' caption='[[6bug]], [[Resolution\|resolution]] 3.27Å' scene=''>
	~~Authors~~:		== Structural highlights ==
			<table><tr><td colspan='2'>[[6bug]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BUG FirstGlance]. <br>
	~~Description~~:		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
	[[Category: ~~Unreleased Structures~~]]		<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=6bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bug OCA], [http://pdbe.org/6bug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bug RCSB], [http://www.ebi.ac.uk/pdbsum/6bug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bug ProSAT]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/DLTC_STRT1 DLTC_STRT1]] Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
			__TOC__
			</StructureSection>
			[[Category: Ma, D]]
			[[Category: Wang, Z]]
			[[Category: Xu, W]]
			[[Category: Membrane protein]]

OCA at 03:58, 25 April 2018

2018-04-25T03:58:05Z

← Older revision		Revision as of 03:58, 25 April 2018
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 6bug is ON HOLD		The entry 6bug is ON HOLD until Paper Publication

	Authors:		Authors:

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

2017-12-20T05:01:46Z

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

← Older revision	Revision as of 05:01, 20 December 2017
(No difference)

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

2017-12-20T05:01:45Z

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

New page

'''Unreleased structure'''

The entry 6bug is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]