6KJG
Crystal structure of PsoF
Summary for 6KJG
| Entry DOI | 10.2210/pdb6kjg/pdb |
| Descriptor | Dual-functional monooxygenase/methyltransferase psoF (2 entities in total) |
| Functional Keywords | metyltransferase, oxidoreductase |
| Biological source | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) |
| Total number of polymer chains | 3 |
| Total formula weight | 125196.12 |
| Authors | Hara, K.,Hashimoto, H.,Matsushita, T.,Tsunematsu, Y.,Watanabe, K. (deposition date: 2019-07-22, release date: 2019-09-18, Last modification date: 2023-11-22) |
| Primary citation | Kishimoto, S.,Tsunematsu, Y.,Matsushita, T.,Hara, K.,Hashimoto, H.,Tang, Y.,Watanabe, K. Functional and Structural Analyses oftrans C-Methyltransferase in Fungal Polyketide Biosynthesis. Biochemistry, 58:3933-3937, 2019 Cited by PubMed Abstract: Biosynthesis of certain fungal polyketide-peptide synthetases involves -methyltransferase activity that adds one or more -adenosyl-l-methionine-derived methyl groups to the carbon framework. The previously reported PsoF-MT, the stand-alone -methyltransferase (MT) from the pseurotin biosynthetic pathway that exists as a domain within a trifunctional didomain enzyme PsoF, was characterized crystallographically and kinetically using mutants with substrate analogs to understand how a -acting -MT works and compare it to known polyketide synthase-associated -MTs. This study identified key active-site residues involved in catalysis and substrate recognition, which led us to propose the mechanism of -methylation and substrate specificity determinants in PsoF-MT. PubMed: 31486637DOI: 10.1021/acs.biochem.9b00702 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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