5azc

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'''Unreleased structure'''
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==Crystal structure of Escherichia coli Lgt in complex with phosphatidylglycerol==
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<StructureSection load='5azc' size='340' side='right' caption='[[5azc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5azc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGT:(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PGT</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5azb|5azb]]</td></tr>
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<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=5azc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azc OCA], [http://pdbe.org/5azc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5azc RCSB], [http://www.ebi.ac.uk/pdbsum/5azc PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 5azc is ON HOLD until Paper Publication
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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>
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Authors: Zhang, X.C., Mao, G., Zhao, Y.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Structure of a protein
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<div class="pdbe-citations 5azc" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Mao, G]]
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[[Category: Zhang, X C]]
[[Category: Zhao, Y]]
[[Category: Zhao, Y]]
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[[Category: Mao, G]]
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[[Category: Complex]]
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[[Category: Zhang, X.C]]
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[[Category: Inhibitor]]
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[[Category: Transferase]]

Revision as of 02:17, 28 January 2016

Crystal structure of Escherichia coli Lgt in complex with phosphatidylglycerol

5azc, resolution 1.90Å

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