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TitleStructure of a eukaryotic cholinephosphotransferase-1 reveals mechanisms of substrate recognition and catalysis.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2753, Year 2023
Publish dateMay 13, 2023
AuthorsLie Wang / Ming Zhou /
PubMed AbstractPhosphatidylcholine (PC) is the most abundant phospholipid in eukaryotic cell membranes. In eukaryotes, two highly homologous enzymes, cholinephosphotransferase-1 (CHPT1) and choline/ethanolamine ...Phosphatidylcholine (PC) is the most abundant phospholipid in eukaryotic cell membranes. In eukaryotes, two highly homologous enzymes, cholinephosphotransferase-1 (CHPT1) and choline/ethanolamine phosphotransferase-1 (CEPT1) catalyze the final step of de novo PC synthesis. CHPT1/CEPT1 joins two substrates, cytidine diphosphate-choline (CDP-choline) and diacylglycerol (DAG), to produce PC, and Mg is required for the reaction. However, mechanisms of substrate recognition and catalysis remain unresolved. Here we report structures of a CHPT1 from Xenopus laevis (xlCHPT1) determined by cryo-electron microscopy to an overall resolution of ~3.2 Å. xlCHPT1 forms a homodimer, and each protomer has 10 transmembrane helices (TMs). The first 6 TMs carve out a cone-shaped enclosure in the membrane in which the catalysis occurs. The enclosure opens to the cytosolic side, where a CDP-choline and two Mg are coordinated. The structures identify a catalytic site unique to eukaryotic CHPT1/CEPT1 and suggest an entryway for DAG. The structures also reveal an internal pseudo two-fold symmetry between TM3-6 and TM7-10, and suggest that CHPT1/CEPT1 may have evolved from their distant prokaryotic ancestors through gene duplication.
External linksNat Commun / PubMed:37179328 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.7 Å
Structure data

28556

8ero

EMDB-28556, PDB-8ero:
Structure of Xenopus cholinephosphotransferase1 in complex with CDP
Method: EM (single particle) / Resolution: 3.2 Å

28557

8erp

EMDB-28557, PDB-8erp:
Structure of Xenopus cholinephosphotransferase1 in complex with CDP-choline
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-LBN:
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / phospholipid*YM

ChemComp-CDP:
CYTIDINE-5'-DIPHOSPHATE

ChemComp-CDC:
[2-CYTIDYLATE-O'-PHOSPHONYLOXYL]-ETHYL-TRIMETHYL-AMMONIUM

Source
  • xenopus laevis (African clawed frog)
KeywordsTRANSFERASE / CDP-APs / phospholipid synthesis

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