5azc

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==Crystal structure of Escherichia coli Lgt in complex with phosphatidylglycerol==
==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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<StructureSection load='5azc' size='340' side='right'caption='[[5azc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== 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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<table><tr><td colspan='2'>[[5azc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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 [https://proteopedia.org/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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.902&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5azc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azc OCA], [https://pdbe.org/5azc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5azc RCSB], [https://www.ebi.ac.uk/pdbsum/5azc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5azc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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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[https://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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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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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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<div class="pdbe-citations 5azc" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Mao, G]]
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[[Category: Escherichia coli K-12]]
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[[Category: Zhang, X C]]
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[[Category: Large Structures]]
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[[Category: Zhao, Y]]
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[[Category: Mao G]]
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[[Category: Complex]]
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[[Category: Zhang XC]]
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[[Category: Inhibitor]]
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[[Category: Zhao Y]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Escherichia coli Lgt in complex with phosphatidylglycerol

PDB ID 5azc

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