5MGZ
Streptomyces Spheroides NovO (8-demethylnovbiocic acid methyltransferase) with SAH
Summary for 5MGZ
| Entry DOI | 10.2210/pdb5mgz/pdb |
| Descriptor | 8-demethylnovobiocic acid C(8)-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | c methyltransferase, novobiocin biosynthesis, sam dependent, transferase |
| Biological source | Streptomyces niveus |
| Total number of polymer chains | 2 |
| Total formula weight | 53435.12 |
| Authors | Chung, C.-W.,Mosley, J.,Sadler, J.C. (deposition date: 2016-11-22, release date: 2017-01-18, Last modification date: 2024-05-08) |
| Primary citation | Sadler, J.C.,Chung, C.H.,Mosley, J.E.,Burley, G.A.,Humphreys, L.D. Structural and Functional Basis of C-Methylation of Coumarin Scaffolds by NovO. ACS Chem. Biol., 12:374-379, 2017 Cited by PubMed Abstract: C-methylation of aromatic small molecules by C-methyltransferases (C-MTs) is an important biological transformation that involves C-C bond formation using S-adenosyl-l-methionine (SAM) as the methyl donor. Here, two advances in the mechanistic understanding of C-methylation of the 8-position of coumarin substrates catalyzed by the C-MT NovO from Streptomyces spheroides are described. First, a crystal structure of NovO reveals the Arg116-Asn117 and His120-Arg121 motifs are essential for coumarin substrate binding. Second, the active-site His120 is responsible for deprotonation of the phenolic 7-hydroxyl group on the coumarin substrate, activating the rate-determining methyl transfer step from SAM. This work expands our mechanistic knowledge of C-MTs, which could be used in the downstream development of engineered biocatalysts for small molecule C-alkylations. PubMed: 28068060DOI: 10.1021/acschembio.6b01053 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
