7XVJ
Crystal structure of CdpNPT in complex with harmol
Summary for 7XVJ
| Entry DOI | 10.2210/pdb7xvj/pdb |
| Descriptor | Cyclic dipeptide N-prenyltransferase, PHOSPHATE ION, 1-methyl-9~{H}-pyrido[3,4-b]indol-7-ol, ... (4 entities in total) |
| Functional Keywords | prenyltransferases, cyclic dipeptide n-prenyltransferase, transferase |
| Biological source | Neosartorya fumigata (Aspergillus fumigatus) |
| Total number of polymer chains | 4 |
| Total formula weight | 185425.32 |
| Authors | Nakashima, Y.,Morita, H. (deposition date: 2022-05-24, release date: 2023-04-05, Last modification date: 2023-11-29) |
| Primary citation | Hamdy, S.A.,Kodama, T.,Nakashima, Y.,Han, X.,Matsui, T.,Morita, H. Enzymatic formation of a prenyl beta-carboline by a fungal indole prenyltransferase. J Nat Med, 76:873-879, 2022 Cited by PubMed Abstract: CdpNPT from Aspergillus fumigatus is a fungal indole prenyltransferase (IPT) with remarkable substrate promiscuity to generate prenylated compounds. Our first investigation of the catalytic potential of CdpNPT against a β-carboline, harmol (1), revealed that the enzyme also accepts 1 as the prenyl acceptor with dimethylallyl diphosphate (DMAPP) as the prenyl donor and selectively prenylates the C-6 position of 1 by the "regular-type" dimethylallylation to produce 6-(3-dimethylallyl)harmol (2). Furthermore, our X-ray crystal structure analysis of the C-His-tagged CdpNPT (38-440) truncated mutant complexed with 1 and docking studies of DMAPP to the crystal structure of the CdpNPT (38-440) mutant suggested that CdpNPT could employ the two-step prenylation system to produce 2. PubMed: 35767141DOI: 10.1007/s11418-022-01635-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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