ArticleThe Journal of biological chemistry2009
Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 61 citations in OpenAlex.
- Preclinical efficacy of a gene therapy forMolecular therapy. Advances · 2026Article
- Structure/function of ATP sulfurylase domain of human 3'-phosphoadenosine 5'-phosphosulfate synthase (hPAPSS).Biochemistry and biophysics reports · 2025Article
- Article
- Identification of a nuclear localization signal in the Plasmodium falciparum CTP: phosphocholine cytidylyltransferase enzyme.Scientific reports · 2020Article
- Interdomain communication in the phosphatidylcholine regulatory enzyme, CCTα, relies on a modular αE helix.The Journal of biological chemistry · 2019Article
- Remodeling of the interdomain allosteric linker upon membrane binding of CCTα pulls its active site close to the membrane surface.The Journal of biological chemistry · 2019Article
- Disease-linked mutations in the phosphatidylcholine regulatory enzyme CCTα impair enzymatic activity and fold stability.The Journal of biological chemistry · 2019Article
- Structural determinants of the catalytic mechanism of Plasmodium CCT, a key enzyme of malaria lipid biosynthesis.Scientific reports · 2018Article
- PCYT1A Regulates Phosphatidylcholine Homeostasis from the Inner Nuclear Membrane in Response to Membrane Stored Curvature Elastic Stress.Developmental cell · 2018Article
- An auto-inhibitory helix in CTP:phosphocholine cytidylyltransferase hijacks the catalytic residue and constrains a pliable, domain-bridging helix pair.The Journal of biological chemistry · 2018Article
- Article
- Structure of a CGI-58 motif provides the molecular basis of lipid droplet anchoring.The Journal of biological chemistry · 2015Article
- Article
- Analysis of the protein domain and domain architecture content in fungi and its application in the search of new antifungal targets.PLoS computational biology · 2014Article
- Mutations disrupting the Kennedy phosphatidylcholine pathway in humans with congenital lipodystrophy and fatty liver disease.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Isoform-specific and protein kinase C-mediated regulation of CTP:phosphoethanolamine cytidylyltransferase phosphorylation.The Journal of biological chemistry · 2014Article
- Structural basis for autoinhibition of CTP:phosphocholine cytidylyltransferase (CCT), the regulatory enzyme in phosphatidylcholine synthesis, by its membrane-binding amphipathic helix.The Journal of biological chemistry · 2014Article
- Mutations in PCYT1A cause spondylometaphyseal dysplasia with cone-rod dystrophy.American journal of human genetics · 2014Article
- Mutations in PCYT1A, encoding a key regulator of phosphatidylcholine metabolism, cause spondylometaphyseal dysplasia with cone-rod dystrophy.American journal of human genetics · 2014Article
- Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain.The EMBO journal · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
ctpphosphocholine cytidylyltransferase (CCT) is the key regulatory enzyme in the synthesis of phosphatidylcholine, the most abundant phospholipid in eukaryotic cell membranes. The CCT-catalyzed transfer of a cytidylyl group from CTP to phosphocholine to form CDP-choline is regulated by a membrane lipid-dependent mechanism imparted by its C-terminal membrane binding domain. We present the first analysis of a crystal structure of a eukaryotic CCT. A deletion construct of rat CCTalpha spanning residues 1-236 (CCT236) lacks the regulatory domain and as a result displays constitutive activity. The 2.2-A structure reveals a CCT236 homodimer in complex with the reaction product, CDP-choline. Each chain is composed of a complete catalytic domain with an intimately associated N-terminal extension, which together with the catalytic domain contributes to the dimer interface. Although the CCT236 structure reveals elements involved in binding cytidine that are conserved with other members of the cytidylyltransferase superfamily, it also features nonconserved active site residues, His-168 and Tyr-173, that make key interactions with the beta-phosphate of CDP-choline. Mutagenesis and kinetic analyses confirmed their role in phosphocholine binding and catalysis. These results demonstrate structural and mechanistic differences in a broadly conserved protein fold across the cytidylyltransferase family. Comparison of the CCT236 structure with those of other nucleotidyltransferases provides evidence for substrate-induced active site loop movements and a disorder-to-order transition of a loop element in the catalytic mechanism.
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