5azb: Difference between revisions
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''' | ==Crystal structure of Escherichia coli Lgt in complex with phosphatidylglycerol and the inhibitor palmitic acid== | ||
<StructureSection load='5azb' size='340' side='right' caption='[[5azb]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5azb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=PGT:(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PGT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5azc|5azc]]</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=5azb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azb OCA], [http://pdbe.org/5azb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5azb RCSB], [http://www.ebi.ac.uk/pdbsum/5azb PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/LGT_ECOLI LGT_ECOLI]] Transfers the N-acyl diglyceride group on what will become the N-terminal cysteine of membrane lipoproteins.<ref>PMID:8051048</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lipoprotein biogenesis is essential for bacterial survival. Phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (Lgt) is an integral membrane enzyme that catalyses the first reaction of the three-step post-translational lipid modification. Deletion of the lgt gene is lethal to most Gram-negative bacteria. Here we present the crystal structures of Escherichia coli Lgt in complex with phosphatidylglycerol and the inhibitor palmitic acid at 1.9 and 1.6 A resolution, respectively. The structures reveal the presence of two binding sites and support the previously reported structure-function relationships of Lgt. Complementation results of lgt-knockout cells with different mutant Lgt variants revealed critical residues, including Arg143 and Arg239, that are essential for diacylglyceryl transfer. Using a GFP-based in vitro assay, we correlated the activities of Lgt with structural observations. Together, the structural and biochemical data support a mechanism whereby substrate and product, lipid-modified lipobox-containing peptide, enter and leave the enzyme laterally relative to the lipid bilayer. | |||
Crystal structure of E. coli lipoprotein diacylglyceryl transferase.,Mao G, Zhao Y, Kang X, Li Z, Zhang Y, Wang X, Sun F, Sankaran K, Zhang XC Nat Commun. 2016 Jan 5;7:10198. doi: 10.1038/ncomms10198. PMID:26729647<ref>PMID:26729647</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5azb" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mao, G]] | |||
[[Category: Zhang, X C]] | |||
[[Category: Zhao, Y]] | [[Category: Zhao, Y]] | ||
[[Category: | [[Category: Complex]] | ||
[[Category: | [[Category: Inhibitor]] | ||
[[Category: Transferase]] | |||
Revision as of 02:19, 28 January 2016
Crystal structure of Escherichia coli Lgt in complex with phosphatidylglycerol and the inhibitor palmitic acid
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