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==Cryo-EM structure of apolipoprotein N-acyltransferase Lnt from E. coli (Apo form)==
<StructureSection load='8b0k' size='340' side='right'caption='[[8b0k]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8b0k]] 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=8B0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B0K 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&#8491;</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=8b0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b0k OCA], [https://pdbe.org/8b0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b0k RCSB], [https://www.ebi.ac.uk/pdbsum/8b0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b0k 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8b0k" 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]]