8gyw

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Current revision (06:44, 3 July 2025) (edit) (undo)
 
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==Structural basis for catalysis of human choline/ethanolamine phosphotransferase (CEPT1) complexed with CDP-choline==
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==Cryo-EM structure of human CEPT1 complexed with CDP-choline==
<StructureSection load='8gyw' size='340' side='right'caption='[[8gyw]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
<StructureSection load='8gyw' size='340' side='right'caption='[[8gyw]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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</table>
</table>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/CEPT1_HUMAN CEPT1_HUMAN] Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP-ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity.<ref>PMID:10191259</ref> <ref>PMID:10893425</ref> <ref>PMID:12216837</ref>
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[https://www.uniprot.org/uniprot/CEPT1_HUMAN CEPT1_HUMAN] Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP-ethanolamine, respectively (PubMed:10191259, PubMed:10893425, PubMed:12216837, PubMed:37137909). Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface (PubMed:10191259, PubMed:10893425, PubMed:12216837). Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity (PubMed:10191259, PubMed:12216837).<ref>PMID:10191259</ref> <ref>PMID:10893425</ref> <ref>PMID:12216837</ref> <ref>PMID:37137909</ref>
== References ==
== References ==
<references/>
<references/>

Current revision

Cryo-EM structure of human CEPT1 complexed with CDP-choline

PDB ID 8gyw

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