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| | <StructureSection load='5azc' size='340' side='right'caption='[[5azc]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5azc' size='340' side='right'caption='[[5azc]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5azc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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> | + | <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> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.902Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5azb|5azb]]</td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lgt, umpA, b2828, JW2796 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=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> |
| - | <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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5azc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [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> |
| - | <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®/PubMed®, 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> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mao, G]] | + | [[Category: Mao G]] |
| - | [[Category: Zhang, X C]] | + | [[Category: Zhang XC]] |
| - | [[Category: Zhao, Y]] | + | [[Category: Zhao Y]] |
| - | [[Category: Complex]]
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| - | [[Category: Inhibitor]]
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| - | [[Category: Transferase]]
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