ArticleNature communications2014
Structural basis for catalysis in a CDP-alcohol phosphotransferase.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 51 citations in OpenAlex.
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- Structural basis for catalysis and selectivity of phospholipid synthesis by eukaryotic choline-phosphotransferase.Nature communications · 2025Article
- The small molecule CBR-5884 inhibits themBio · 2024Article
- Innovations in Antifungal Drug Discovery among Cell Envelope Synthesis Enzymes through Structural Insights.Journal of fungi (Basel, Switzerland) · 2024Review
- Architects of the membrane: structures of eukaryotic choline phosphotransferase 1 and choline/ethanolamine phosphotransferase 1.Nature structural & molecular biology · 2023Article
- Multiple approaches of cellular metabolism define the bacterial ancestry of mitochondria.Science advances · 2023Article
- Structure of a eukaryotic cholinephosphotransferase-1 reveals mechanisms of substrate recognition and catalysis.Nature communications · 2023Article
- Structural basis for catalysis of human choline/ethanolamine phosphotransferase 1.Nature communications · 2023Article
- Evolution of Enterococcus faecium in Response to a Combination of Daptomycin and Fosfomycin Reveals Distinct and Diverse Adaptive Strategies.Antimicrobial agents and chemotherapy · 2022Article
- PE_PGRS3 ensures provision of the vital phospholipids cardiolipin and phosphatidylinositols by promoting the interaction betweenVirulence · 2021Article
- Crystal structures of phosphatidyl serine synthase PSS reveal the catalytic mechanism of CDP-DAG alcohol O-phosphatidyl transferases.Nature communications · 2021Article
- MENSAdb: a thorough structural analysis of membrane protein dimers.Database : the journal of biological databases and curation · 2021Article
- Mapping the Substrate-Binding Sites in the Phosphatidylserine Synthase inFrontiers in cellular and infection microbiology · 2021Article
- The phosphatidylglycerol phosphate synthase PgsA utilizes a trifurcated amphipathic cavity for catalysis at the membrane-cytosol interface.Current research in structural biology · 2021Article
- Structural and Functional Characterization of Phosphatidylinositol-Phosphate Biosynthesis in Mycobacteria.Journal of molecular biology · 2020Article
- Mutations inAntimicrobial agents and chemotherapy · 2019Article
- Interfaces Between Alpha-helical Integral Membrane Proteins: Characterization, Prediction, and Docking.Computational and structural biotechnology journal · 2019Article
- Structure ofCommunications biology · 2019Article
- Structural basis for catalysis at the membrane-water interface.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Lipid topogenesis--35years on.Biochimica et biophysica acta · 2016Review
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
The CDP-alcohol phosphotransferase (CDP-AP) family of integral membrane enzymes catalyses the transfer of a substituted phosphate group from a CDP-linked donor to an alcohol acceptor. This is an essential reaction for phospholipid biosynthesis across all kingdoms of life, and it is catalysed solely by CDP-APs. Here we report the 2.0 Å resolution crystal structure of a representative CDP-AP from Archaeoglobus fulgidus. The enzyme (AF2299) is a homodimer, with each protomer consisting of six transmembrane helices and an N-terminal cytosolic domain. A polar cavity within the membrane accommodates the active site, lined with the residues from an absolutely conserved CDP-AP signature motif (D(1)xxD(2)G(1)xxAR...G(2)xxxD(3)xxxD(4)). Structures in the apo, CMP-bound, CDP-bound and CDP-glycerol-bound states define functional roles for each of these eight conserved residues and allow us to propose a sequential, base-catalysed mechanism universal for CDP-APs, in which the fourth aspartate (D4) acts as the catalytic base.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.