5XHQ

Apolipoprotein N-acyl Transferase

5XHQ の概要

• エントリーDOI: 10.2210/pdb5xhq/pdb
• 分子名称: Apolipoprotein N-acyltransferase, heptyl 1-thio-beta-D-glucopyranoside, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: nitrilase post-lipidation lipoprotein, transferase
• 由来する生物種: Escherichia coli (strain K12)
• 細胞内の位置: Cell inner membrane ; Multi- pass membrane protein : P23930
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 116411.34

構造登録者

Yingzhi, X.,Yong, X.,Guangyuan, L.,Fei, S. (登録日: 2017-04-23, 公開日: 2017-07-26, 最終更新日: 2024-10-23)

主引用文献

Lu, G.,Xu, Y.,Zhang, K.,Xiong, Y.,Li, H.,Cui, L.,Wang, X.,Lou, J.,Zhai, Y.,Sun, F.,Zhang, X.C.
Crystal structure of E. coli apolipoprotein N-acyl transferase
Nat Commun, 8:15948-15948, 2017

PubMed Abstract: In Gram-negative bacteria, lipid modification of proteins is catalysed in a three-step pathway. Apolipoprotein N-acyl transferase (Lnt) catalyses the third step in this pathway, whereby it transfers an acyl chain from a phospholipid to the amine group of the N-terminal cysteine residue of the apolipoprotein. Here, we report the 2.6-Å crystal structure of Escherichia coli Lnt. This enzyme contains an exo-membrane nitrilase domain fused to a transmembrane (TM) domain. The TM domain of Lnt contains eight TM helices which form a membrane-embedded cavity with a lateral opening and a periplasmic exit. The nitrilase domain is located on the periplasmic side of the membrane, with its catalytic cavity connected to the periplasmic exit of the TM domain. An amphipathic lid loop from the nitrilase domain interacts with the periplasmic lipid leaflet, forming an interfacial entrance from the lipid bilayer to the catalytic centre for both the lipid donor and acceptor substrates.

PubMed: 28885614
DOI: 10.1038/ncomms15948

実験手法

X-RAY DIFFRACTION (2.587 Å)