8b0o
From Proteopedia
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(New page: '''Unreleased structure''' The entry 8b0o is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure apolipoprotein N-acyltransferase Lnt from E.coli in complex with FP3== | |
| + | <StructureSection load='8b0o' size='340' side='right'caption='[[8b0o]], [[Resolution|resolution]] 3.02Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8b0o]] 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=8B0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B0O FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.02Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OJF:[(2~{R})-3-[(2~{R})-3-[[(2~{R})-1-[[(2~{R})-1-[[(2~{R})-6-[(2-aminophenyl)carbonylamino]-1-azanyl-1-oxidanylidene-hexan-2-yl]amino]-3-oxidanyl-1-oxidanylidene-propan-2-yl]amino]-3-oxidanyl-1-oxidanylidene-propan-2-yl]amino]-2-(hexadecanoylamino)-3-oxidanylidene-propyl]sulfanyl-2-hexadecanoyloxy-propyl]+hexadecanoate'>OJF</scene></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=8b0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b0o OCA], [https://pdbe.org/8b0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b0o RCSB], [https://www.ebi.ac.uk/pdbsum/8b0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b0o ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LNT_ECOLI LNT_ECOLI] Transfers the fatty acyl group on membrane lipoproteins. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacterial lipoproteins (BLPs) decorate the surface of membranes in the cell envelope. They function in membrane assembly and stability, as enzymes, and in transport. The final enzyme in the BLP synthesis pathway is the apolipoprotein N-acyltransferase, Lnt, which is proposed to act by a ping-pong mechanism. Here, we use x-ray crystallography and cryo-electron microscopy to chart the structural changes undergone during the progress of the enzyme through the reaction. We identify a single active site that has evolved to bind, individually and sequentially, substrates that satisfy structural and chemical criteria to position reactive parts next to the catalytic triad for reaction. This study validates the ping-pong mechanism, explains the molecular bases for Lnt's substrate promiscuity, and should facilitate the design of antibiotics with minimal off-target effects. | ||
| - | + | Structure snapshots reveal the mechanism of a bacterial membrane lipoprotein N-acyltransferase.,Smithers L, Degtjarik O, Weichert D, Huang CY, Boland C, Bowen K, Oluwole A, Lutomski C, Robinson CV, Scanlan EM, Wang M, Olieric V, Shalev-Benami M, Caffrey M Sci Adv. 2023 Jun 30;9(26):eadf5799. doi: 10.1126/sciadv.adf5799. Epub 2023 Jun , 30. PMID:37390210<ref>PMID:37390210</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8b0o" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Boland C]] | ||
| + | [[Category: Caffrey M]] | ||
| + | [[Category: Degtjarik O]] | ||
| + | [[Category: Shalev Benami M]] | ||
| + | [[Category: Smithers L]] | ||
Current revision
Cryo-EM structure apolipoprotein N-acyltransferase Lnt from E.coli in complex with FP3
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