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Crystal structure of E. coli apolipoprotein N-acyl transferase

Author

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  • Guangyuan Lu

    (National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences
    School of Life Sciences, University of Chinese Academy of Sciences)

  • Yingzhi Xu

    (National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences
    Present address: Beijing Key Laboratory of Novel Technique for Combined Vaccine, Beijing Minhai Biotechnology Co. Ltd, 35 Simiao Road, Beijing 102600, China)

  • Kai Zhang

    (National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences
    Present address: Medical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge CB2 0QH, UK)

  • Yong Xiong

    (Yale University)

  • He Li

    (National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences)

  • Lei Cui

    (National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences)

  • Xianping Wang

    (National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences
    School of Life Sciences, University of Chinese Academy of Sciences)

  • Jizhong Lou

    (National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences
    School of Life Sciences, University of Chinese Academy of Sciences)

  • Yujia Zhai

    (National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences)

  • Fei Sun

    (National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences
    School of Life Sciences, University of Chinese Academy of Sciences)

  • Xuejun C. Zhang

    (National Laboratory of Macromolecules, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences
    School of Life Sciences, University of Chinese Academy of Sciences)

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.

Suggested Citation

  • Guangyuan Lu & Yingzhi Xu & Kai Zhang & Yong Xiong & He Li & Lei Cui & Xianping Wang & Jizhong Lou & Yujia Zhai & Fei Sun & Xuejun C. Zhang, 2017. "Crystal structure of E. coli apolipoprotein N-acyl transferase," Nature Communications, Nature, vol. 8(1), pages 1-8, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15948
    DOI: 10.1038/ncomms15948
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