9K2F
Crystal Structure of CyaF/SAH in open conformational state
Summary for 9K2F
| Entry DOI | 10.2210/pdb9k2f/pdb |
| Descriptor | CyaF, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total) |
| Functional Keywords | cyanogramide, n-methyltransferase, substrate promiscuity, open conformation, biosynthetic protein |
| Biological source | Actinoalloteichus caeruleus (Streptomyces caeruleus) |
| Total number of polymer chains | 2 |
| Total formula weight | 57180.37 |
| Authors | Chen, R.J.,Zhang, L.P.,Zhu, Y.G.,Zhang, C.S. (deposition date: 2024-10-17, release date: 2025-10-22, Last modification date: 2026-05-13) |
| Primary citation | Chen, R.,Zhang, Q.,Zhang, L.,Fang, C.,Zhu, H.,Zhu, W.,Zhang, C.,Zhu, Y. Biochemical and Structural Insights of the N -Methyltransferase CyaF in Cyanogramide Biosynthesis. J.Nat.Prod., 88:715-722, 2025 Cited by PubMed Abstract: -Methyltransferases involved in indole methylation have seldom been discovered in natural product biosynthesis. This study focuses on the enzyme CyaF, which catalyzes a critical -methylation step of indole in the β-carboline skeleton during cyanogramide biosynthesis. Seven β-carboline analogues (-) were isolated from the recombinant strain YF11/, including three new compounds (-). assays revealed CyaF's substrate flexibility. The crystal structure of the CyaF/-adenosyl-L-homocysteine (SAH) complex, combined with the AlphaFold-predicted model and site-directed mutagenesis, elucidated the catalytic mechanism and structural features that enable CyaF to accommodate diverse substrates, highlighting its potential for biocatalytic applications. PubMed: 40053516DOI: 10.1021/acs.jnatprod.4c01391 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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