8U0Z
CRYSTAL STRUCTURE OF THE OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE DOMAIN OF Coffea arabica UMP SYNTHASE
Summary for 8U0Z
| Entry DOI | 10.2210/pdb8u0z/pdb |
| Descriptor | Uridine 5'-monophosphate synthase, 1,2-ETHANEDIOL, ANY 5'-MONOPHOSPHATE NUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | coffea arabica, orotidine 5'-monophosphate decarboxylase, lyase |
| Biological source | Coffea arabica (coffee) |
| Total number of polymer chains | 2 |
| Total formula weight | 57804.42 |
| Authors | Hinojosa-Cruz, A.,Diaz-Vilchis, A.,Gonzalez-Segura, L. (deposition date: 2023-08-29, release date: 2024-01-17, Last modification date: 2024-01-24) |
| Primary citation | Hinojosa-Cruz, A.,Diaz-Sanchez, A.G.,Diaz-Vilchis, A.,Gonzalez-Segura, L. Structural and functional properties of uridine 5'-monophosphate synthase from Coffea arabica. Int.J.Biol.Macromol., 259:129226-129226, 2024 Cited by PubMed Abstract: In higher eukaryotes and plants, the last two sequential steps in the de novo biosynthesis of uridine 5'-monophosphate (UMP) are catalyzed by a bifunctional natural chimeric protein called UMP synthase (UMPS). In higher plants, UMPS consists of two naturally fused enzymes: orotate phosphoribosyltransferase (OPRTase) at N-terminal and orotidine-5'-monophosphate decarboxylase (ODCase) at C-terminal. In this work, we obtained the full functional recombinant protein UMPS from Coffea arabica (CaUMPS) and studied its structure-function relationships. A biochemical and structural characterization of a plant UMPS with its two functional domains is described together with the presentation of the first crystal structure of a plant ODCase at 1.4 Å resolution. The kinetic parameters measured of CaOPRTase and CaODCase domains were comparable to those reported. The crystallographic structure revealed that CaODCase is a dimer that conserves the typical fold observed in other ODCases from prokaryote and eukaryote with a 1-deoxy-ribofuranose-5'-phosphate molecule bound in the active site of one subunit induced a closed conformation. Our results add to the knowledge of one of the key enzymes of the de novo biosynthesis of pyrimidines in plant metabolism and open the door to future applications. PubMed: 38184030DOI: 10.1016/j.ijbiomac.2024.129226 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.399 Å) |
Structure validation
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