5n6h: Difference between revisions
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<StructureSection load='5n6h' size='340' side='right'caption='[[5n6h]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='5n6h' size='340' side='right'caption='[[5n6h]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5n6h]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5n6h]] is a 2 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=5N6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N6H FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5n6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n6h OCA], [https://pdbe.org/5n6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n6h RCSB], [https://www.ebi.ac.uk/pdbsum/5n6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n6h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LNT_ECOLI LNT_ECOLI] Transfers the fatty acyl group on membrane lipoproteins. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bailey | [[Category: Bailey J]] | ||
[[Category: Boland | [[Category: Boland C]] | ||
[[Category: Caffrey | [[Category: Caffrey M]] | ||
[[Category: Howe | [[Category: Howe N]] | ||
[[Category: Huang | [[Category: Huang C-Y]] | ||
[[Category: Olieric | [[Category: Olieric V]] | ||
[[Category: Vogeley | [[Category: Vogeley L]] | ||
[[Category: Wang | [[Category: Wang M]] | ||
[[Category: Weichert | [[Category: Weichert D]] | ||
[[Category: Wiktor | [[Category: Wiktor M]] | ||
Latest revision as of 15:29, 15 November 2023
Structure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coliStructure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coli
Structural highlights
FunctionLNT_ECOLI Transfers the fatty acyl group on membrane lipoproteins. Publication Abstract from PubMedLipoproteins serve essential roles in the bacterial cell envelope. The posttranslational modification pathway leading to lipoprotein synthesis involves three enzymes. All are potential targets for the development of new antibiotics. Here we report the crystal structure of the last enzyme in the pathway, apolipoprotein N-acyltransferase, Lnt, responsible for adding a third acyl chain to the lipoprotein's invariant diacylated N-terminal cysteine. Structures of Lnt from Pseudomonas aeruginosa and Escherichia coli have been solved; they are remarkably similar. Both consist of a membrane domain on which sits a globular periplasmic domain. The active site resides above the membrane interface where the domains meet facing into the periplasm. The structures are consistent with the proposed ping-pong reaction mechanism and suggest plausible routes by which substrates and products enter and leave the active site. While Lnt may present challenges for antibiotic development, the structures described should facilitate design of therapeutics with reduced off-target effects. Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis.,Wiktor M, Weichert D, Howe N, Huang CY, Olieric V, Boland C, Bailey J, Vogeley L, Stansfeld PJ, Buddelmeijer N, Wang M, Caffrey M Nat Commun. 2017 Jul 4;8:15952. doi: 10.1038/ncomms15952. PMID:28675161[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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