5dep - Revision history

OCA at 12:24, 6 March 2024

OCA — Wed, 06 Mar 2024 12:24:09 GMT

←Older revision		Revision as of 12:24, 6 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5dep]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PA7 Pseudomonas aeruginosa PA7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DEP FirstGlance]. <br>		<table><tr><td colspan='2'>[[5dep]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PA7 Pseudomonas aeruginosa PA7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DEP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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]] 2.16Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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=5dep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dep OCA], [https://pdbe.org/5dep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dep RCSB], [https://www.ebi.ac.uk/pdbsum/5dep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dep 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=5dep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dep OCA], [https://pdbe.org/5dep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dep RCSB], [https://www.ebi.ac.uk/pdbsum/5dep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dep ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/LPXA_PSEA7 LPXA_PSEA7] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.		[https://www.uniprot.org/uniprot/LPXA_PSEA7 LPXA_PSEA7] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	In Gram-negative bacteria, the first step of lipid A biosynthesis is catalyzed by UDP-N-acetylglucosamine acyltransferase (LpxA) through the transfer of a R-3-hydroxyacyl chain from the acyl carrier protein (ACP) to the 3-hydroxyl group of UDP-GlcNAc. Previous studies suggest that LpxA is a critical determinant of the acyl chain length found in lipid A, which varies among species of bacteria. In Escherichia coli and Leptospira interrogans, LpxA prefers to incorporate longer R-3-hydroxyacyl chains (C14 and C12, respectively), whereas in Pseudomonas aeruginosa, the enzyme is selective for R-3-hydroxydecanoyl, a 10-hydrocarbon long acyl chain. We now report three P. aeruginosa LpxA crystal structures: apo protein, substrate complex with UDP-GlcNAc, and product complex with UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc. A comparison between the apo form and complexes identifies key residues that position UDP-GlcNAc appropriately for catalysis and supports the role of catalytic His121 in activating the UDP-GlcNAc 3-hydroxyl group for nucleophilic attack during the reaction. The product-complex structure, for the first time, offers structural insights into how Met169 serves to constrain the length of the acyl chain and thus functions as the so-called hydrocarbon ruler. Furthermore, compared with ortholog LpxA structures, the purported oxyanion hole, formed by the backbone amide group of Gly139, displays a different conformation in P. aeruginosa LpxA, which suggests flexibility of this structural feature important for catalysis and the potential need for substrate-induced conformational change in catalysis. Taken together, the three structures provide valuable insights into P. aeruginosa LpxA catalysis and substrate specificity as well as templates for future inhibitor discovery.
-
-	Structures of Pseudomonas aeruginosa LpxA Reveal the Basis for Its Substrate Selectivity.,Smith EW, Zhang X, Behzadi C, Andrews LD, Cohen F, Chen Y Biochemistry. 2015 Sep 29;54(38):5937-48. doi: 10.1021/acs.biochem.5b00720. Epub , 2015 Sep 18. PMID:26352800<ref>PMID:26352800</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5dep" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[UDP-N-acetylglucosamine acyltransferase\|UDP-N-acetylglucosamine acyltransferase]]		*[[UDP-N-acetylglucosamine acyltransferase\|UDP-N-acetylglucosamine acyltransferase]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:32, 21 June 2023

OCA — Wed, 21 Jun 2023 10:32:31 GMT

←Older revision		Revision as of 10:32, 21 June 2023
Line 1:		Line 1:

	==Structure of Pseudomonas aeruginosa LpxA in complex with UDP-GlcNAc==		==Structure of Pseudomonas aeruginosa LpxA in complex with UDP-GlcNAc==
-	<StructureSection load='5dep' size='340' side='right' caption='[[5dep]], [[Resolution\|resolution]] 2.16Å' scene=''>	+	<StructureSection load='5dep' size='340' side='right'caption='[[5dep]], [[Resolution\|resolution]] 2.16Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5dep]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Psea7 Psea7~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DEP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5DEP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5dep]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PA7 Pseudomonas aeruginosa PA7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DEP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5dem\|5dem]], [[5dg3\|5dg3]]</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=5dep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dep OCA], [https://pdbe.org/5dep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dep RCSB], [https://www.ebi.ac.uk/pdbsum/5dep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dep ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lpxA, PSPA7_1495 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381754 PSEA7])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.129 2.3.1.129] </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=5dep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dep OCA], [~~http~~://pdbe.org/5dep PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5dep RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5dep PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5dep ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/LPXA_PSEA7 LPXA_PSEA7]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.	+	[https://www.uniprot.org/uniprot/LPXA_PSEA7 LPXA_PSEA7] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 5dep" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5dep" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[UDP-N-acetylglucosamine acyltransferase\|UDP-N-acetylglucosamine acyltransferase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Psea7~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Chen, Y~~]]	+	[[Category: Pseudomonas aeruginosa PA7]]
-	[[Category: ~~Smith, E W~~]]	+	[[Category: Chen Y]]
-	[[Category: ~~Acyltransferase catalytic domain]]~~	+	[[Category: Smith EW]]
-	~~[[Category: Fatty acid]]~~	+
-	~~[[Category: Hydrocarbon ruler]]~~	+
-	~~[[Category: Lipid some]]~~	+
-	~~[[Category: Substrate specificity]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Uridine diphosphate n-acetylglucosamine~~]]	+

OCA at 17:21, 16 November 2017

OCA — Thu, 16 Nov 2017 17:21:00 GMT

←Older revision		Revision as of 17:21, 16 November 2017
Line 1:		Line 1:
		+
	==Structure of Pseudomonas aeruginosa LpxA in complex with UDP-GlcNAc==		==Structure of Pseudomonas aeruginosa LpxA in complex with UDP-GlcNAc==
	<StructureSection load='5dep' size='340' side='right' caption='[[5dep]], [[Resolution\|resolution]] 2.16Å' scene=''>		<StructureSection load='5dep' size='340' side='right' caption='[[5dep]], [[Resolution\|resolution]] 2.16Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5dep]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DEP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5dep]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Psea7 Psea7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DEP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5dem\|5dem]], [[5dg3\|5dg3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5dem\|5dem]], [[5dg3\|5dg3]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lpxA, PSPA7_1495 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381754 PSEA7])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.129 2.3.1.129] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.129 2.3.1.129] </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=5dep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dep OCA], [http://pdbe.org/5dep PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dep RCSB], [http://www.ebi.ac.uk/pdbsum/5dep PDBsum]</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=5dep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dep OCA], [http://pdbe.org/5dep PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dep RCSB], [http://www.ebi.ac.uk/pdbsum/5dep PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dep ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 23:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Psea7]]
	[[Category: Chen, Y]]		[[Category: Chen, Y]]
	[[Category: Smith, E W]]		[[Category: Smith, E W]]

OCA at 06:31, 30 September 2015

OCA — Wed, 30 Sep 2015 06:31:22 GMT

←Older revision		Revision as of 06:31, 30 September 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Structure of Pseudomonas aeruginosa LpxA in complex with UDP-GlcNAc==
		+	<StructureSection load='5dep' size='340' side='right' caption='[[5dep]], [[Resolution\|resolution]] 2.16Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5dep]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DEP FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5dem\|5dem]], [[5dg3\|5dg3]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.129 2.3.1.129] </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=5dep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dep OCA], [http://pdbe.org/5dep PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dep RCSB], [http://www.ebi.ac.uk/pdbsum/5dep PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LPXA_PSEA7 LPXA_PSEA7]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In Gram-negative bacteria, the first step of lipid A biosynthesis is catalyzed by UDP-N-acetylglucosamine acyltransferase (LpxA) through the transfer of a R-3-hydroxyacyl chain from the acyl carrier protein (ACP) to the 3-hydroxyl group of UDP-GlcNAc. Previous studies suggest that LpxA is a critical determinant of the acyl chain length found in lipid A, which varies among species of bacteria. In Escherichia coli and Leptospira interrogans, LpxA prefers to incorporate longer R-3-hydroxyacyl chains (C14 and C12, respectively), whereas in Pseudomonas aeruginosa, the enzyme is selective for R-3-hydroxydecanoyl, a 10-hydrocarbon long acyl chain. We now report three P. aeruginosa LpxA crystal structures: apo protein, substrate complex with UDP-GlcNAc, and product complex with UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc. A comparison between the apo form and complexes identifies key residues that position UDP-GlcNAc appropriately for catalysis and supports the role of catalytic His121 in activating the UDP-GlcNAc 3-hydroxyl group for nucleophilic attack during the reaction. The product-complex structure, for the first time, offers structural insights into how Met169 serves to constrain the length of the acyl chain and thus functions as the so-called hydrocarbon ruler. Furthermore, compared with ortholog LpxA structures, the purported oxyanion hole, formed by the backbone amide group of Gly139, displays a different conformation in P. aeruginosa LpxA, which suggests flexibility of this structural feature important for catalysis and the potential need for substrate-induced conformational change in catalysis. Taken together, the three structures provide valuable insights into P. aeruginosa LpxA catalysis and substrate specificity as well as templates for future inhibitor discovery.

-	~~The entry 5dep is ON HOLD~~	+	Structures of Pseudomonas aeruginosa LpxA Reveal the Basis for Its Substrate Selectivity.,Smith EW, Zhang X, Behzadi C, Andrews LD, Cohen F, Chen Y Biochemistry. 2015 Sep 29;54(38):5937-48. doi: 10.1021/acs.biochem.5b00720. Epub , 2015 Sep 18. PMID:26352800<ref>PMID:26352800</ref>

-	~~Authors: Smith~~, E.W.~~, Chen, Y~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Structure of Pseudomonas aeruginosa LpxA in complex with UDP~~-~~GlcNAc~~	+	<div class="pdbe-citations 5dep" style="background-color:#fffaf0;"></div>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Chen, Y]]		[[Category: Chen, Y]]
-	[[Category: Smith, E.W]]	+	[[Category: Smith, E W]]
		+	[[Category: Acyltransferase catalytic domain]]
		+	[[Category: Fatty acid]]
		+	[[Category: Hydrocarbon ruler]]
		+	[[Category: Lipid some]]
		+	[[Category: Substrate specificity]]
		+	[[Category: Transferase]]
		+	[[Category: Uridine diphosphate n-acetylglucosamine]]

OCA: Protected "5dep" [edit=sysop:move=sysop]

OCA — Wed, 02 Sep 2015 11:33:26 GMT

Protected "5dep" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:33, 2 September 2015

OCA: New page: '''Unreleased structure''' The entry 5dep is ON HOLD Authors: Smith, E.W., Chen, Y. Description: Structure of Pseudomonas aeruginosa LpxA in complex with UDP-GlcNAc [[Category: Unrelea...

OCA — Wed, 02 Sep 2015 11:33:25 GMT

New page: '''Unreleased structure''' The entry 5dep is ON HOLD Authors: Smith, E.W., Chen, Y. Description: Structure of Pseudomonas aeruginosa LpxA in complex with UDP-GlcNAc [[Category: Unrelea...

New page

'''Unreleased structure'''

The entry 5dep is ON HOLD

Authors: Smith, E.W., Chen, Y.

Description: Structure of Pseudomonas aeruginosa LpxA in complex with UDP-GlcNAc
[[Category: Unreleased Structures]]
[[Category: Chen, Y]]
[[Category: Smith, E.W]]