8B0K

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

8B0K の概要

• エントリーDOI: 10.2210/pdb8b0k/pdb
• EMDBエントリー: 15786
• 分子名称: Apolipoprotein N-acyltransferase (1 entity in total)
• 機能のキーワード: lnt, apolipoprotein n-acyltransferase, bacterial lipoprotein, transferase, cryo-em
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59280.77

構造登録者

Degtjarik, O.,Smithers, L.,Boland, C.,Caffrey, M.,Shalev Benami, M. (登録日: 2022-09-07, 公開日: 2023-07-12, 最終更新日: 2024-07-24)

主引用文献

Smithers, L.,Degtjarik, O.,Weichert, D.,Huang, C.Y.,Boland, C.,Bowen, K.,Oluwole, A.,Lutomski, C.,Robinson, C.V.,Scanlan, E.M.,Wang, M.,Olieric, V.,Shalev-Benami, M.,Caffrey, M.
Structure snapshots reveal the mechanism of a bacterial membrane lipoprotein N -acyltransferase.
Sci Adv, 9:eadf5799-eadf5799, 2023

PubMed Abstract: 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 -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.

PubMed: 37390210
DOI: 10.1126/sciadv.adf5799

実験手法

ELECTRON MICROSCOPY (3 Å)