9QCJ
Crystal structure of PhoC wild type acid phosphatase
Summary for 9QCJ
| Entry DOI | 10.2210/pdb9qcj/pdb |
| Descriptor | Major phosphate-irrepressible acid phosphatase, PHOSPHATE ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | acid phosphatase, biosynthetic protein |
| Biological source | Morganella morganii |
| Total number of polymer chains | 3 |
| Total formula weight | 81614.49 |
| Authors | Levy, C.W.,Ortmayer, M. (deposition date: 2025-03-04, release date: 2026-01-14, Last modification date: 2026-01-28) |
| Primary citation | Meng, Q.,Benckendorff, C.,Morrill, C.,Zhuo, Y.,Egerstrom, A.,Ni Cheallaigh, A.,Derrington, S.R.,Obexer, R.,Ortmayer, M.,Levy, C.W.,Finnigan, J.D.,Charnock, S.J.,Turner, N.J.,Miller, G.J.,Lovelock, S.L. Enzymatic synthesis of key RNA therapeutic building blocks using simple phosphate donors. Nat Commun, 17:622-622, 2025 Cited by PubMed Abstract: The rapid emergence of RNA therapeutics has highlighted the need for more efficient, scalable and sustainable methods for their manufacture. Biocatalytic approaches hold particular promise, but rely on a secure, sustainable and low-cost supply of nucleoside triphosphate (NTP) building blocks, including those containing chemical modifications. Here we report the development of a biocatalytic approach and engineered enzymes to convert widely available nucleosides into NTPs featuring pharmaceutically relevant modifications using inexpensive phosphate donors. Importantly our strategy obviates the need for ATP as a phosphate donor that complicates NTP isolation using existing methods. To showcase the utility of our approach, we employ an engineered acid phosphatase, polyphosphate kinase and acetate kinase to produce 2'-O-methoxyethyl-ATP (2'-MOE-ATP) and 2'-fluoro-ATP, key building blocks of commercial therapeutics. Finally, we show that crude NTPs from our process can be used directly in enzymatic oligonucleotide synthesis, obviating the need for costly NTP isolation or purification steps. PubMed: 41402308DOI: 10.1038/s41467-025-67366-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.24 Å) |
Structure validation
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