8b0k

Cryo-EM structure of apolipoprotein N-acyltransferase Lnt from E. coli (Apo form)

spinqualitylabelsall models 8b0k, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8b0k is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LNT_ECOLI Transfers the fatty acyl group on membrane lipoproteins. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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