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Nat Commun. 2017 Jul 4;8:15948. doi: 10.1038/ncomms15948.

Crystal structure of E. coli apolipoprotein N-acyl transferase.

Lu G1,2, Xu Y1, Zhang K1, Xiong Y3, Li H1, Cui L1, Wang X1,2, Lou J1,2, Zhai Y1, Sun F1,2, Zhang XC1,2.

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National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.
School of Life Sciences, University of Chinese Academy of Sciences, 19 Yuquan Road, Beijing 100049, China.
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06411, USA.


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.

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