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Structural basis for substrate selectivity and evolutionary insights into human choline phosphotransferase 1.

Yonglin He1, Yufan Yang1, Meng Yang1

  • 1Department of Cardiology, The First Affiliated Hospital of USTC, MOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, 230027, China.

Biochemical and Biophysical Research Communications
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PubMed
Summary

Researchers elucidated the structure of human choline phosphotransferase 1 (hCHPT1), revealing key residues for substrate selectivity in phospholipid synthesis. This finding offers evolutionary insights into enzyme adaptation.

Keywords:
Biochemical characterizationsCholine phosphotransferase 1Choline/ethanolamine phosphotransferase 1Cryo-EMSequence alignmentSubstrate selectivity

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Evolution

Background:

  • Phosphatidylcholine (PC) and phosphatidylethanolamine (PE) are crucial for eukaryotic membrane integrity.
  • The Kennedy pathway, involving choline phosphotransferase 1 (CHPT1) and choline ethanolamine phosphotransferase 1 (CEPT1), synthesizes these phospholipids.
  • The substrate selectivity mechanism of CHPT1 versus CEPT1 is not well understood.

Purpose of the Study:

  • To determine the cryo-EM structure of human CHPT1 (hCHPT1).
  • To identify the structural basis for substrate selectivity in CHPT1.
  • To explore evolutionary aspects of phospholipid synthase adaptation.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the 3.7 Å structure of hCHPT1.
  • Structural and sequence analyses of hCHPT1.
  • Biochemical characterization of hCHPT1.
  • Cross-species sequence alignment.

Main Results:

  • The hCHPT1 structure reveals a homodimer with distinct N-terminal, catalytic, and dimerization domains.
  • Specific residues in the catalytic domain were identified as critical for substrate selectivity.
  • Ovipara CHPT1 shares conserved residues with CEPT1, suggesting potential bifunctionality.

Conclusions:

  • The study elucidates the structural basis for substrate selectivity between CHPT1 and CEPT1.
  • Identified residues provide insights into the mechanism of PC synthesis by CHPT1.
  • Conserved residues suggest evolutionary adaptation in phospholipid synthesis pathways.