Structural Research of CDP-Alcohol Phosphotransferases
CDP-alcohol phosphotransferases (CDP-APs) are a class of enzymes that play a critical role in the biosynthesis of phospholipids, which are essential components of cell membranes. X-ray crystallography is a powerful tool for determining the three-dimensional structures of proteins and other biomolecules. In recent years, significant progress has been made in the structure determination of CDP-APs, providing valuable insights into the catalytic mechanism and substrate specificity of these enzymes.
The crystal structure of a bifunctional enzyme that comprises a cytoplasmic nucleotidyltransferase domain (IPCT) fused with a membrane CDP-AP domain (DIPPS). The bifunctional protein dimerizes through the DIPPS domains, which constitute six transmembrane α-helices, thereby creating a crucial and comprehensive channel for the efficient transportation of vital biomolecules across the membrane. The active site cavity, which is hydrophilic and open to the cytoplasm, contains a magnesium ion that is encircled by four highly conserved aspartate residues from helices TM2 and TM3, thereby playing a crucial role in enzymatic activity and catalysis.
Figure 1. X-ray structure of IPCT/DIPPS. (Nogly P, et al., 2014)
| Protein | Organism | Method | Resolution | PDB Entry ID |
| AF2299 CDP-alcohol phosphotransferase w. bound CMP (expressed in E. coli) | Archaeoglobus fulgidus | X-ray diffraction | 1.90 Å | 4O6M |
| CDP-alcohol phosphotransferase domain (DIPPS) with fused nucleotidyltransferase domain (expressed in E. coli) | Archaeoglobus fulgidus | X-ray diffraction | 2.66 Å | 4MND |
| Phosphatidylinositol-phosphate synthase with bound CDP-diacylglycerol (expressed in E. coli) | Renibacterium Salmoninarum | X-ray diffraction | 2.50 Å | 5D91 |
Table 1. Structural Research of CDP-Alcohol Phosphotransferases.
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Creative Biostructure is an industry-leading structural analysis service provider that specializes in the elucidation of complex molecular structures. With cutting-edge technologies and advanced equipment, we are uniquely positioned to provide unparalleled structural analysis services to our clients. With our expertise in the field of membrane proteins, we are committed to supporting the advancement of research in this area by providing top-notch structural biology services. We welcome all researchers and institutions to contact us for inquiries and consultations. Contact us today to learn more about how we can help advance your research.
References
- Sciara G, et al. Structural basis for catalysis in a CDP-alcohol phosphotransferase. Nature Communications. 2014, 5(1): 4068.
- Nogly P, et al. X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into its catalytic mechanism. Nature Communications. 2014, 5(1): 4169.
- Clarke O B, et al. Structural basis for phosphatidylinositol-phosphate biosynthesis. Nature Communications. 2015, 6(1): 8505.
