Summary for 6ZRY
| Entry DOI | 10.2210/pdb6zry/pdb |
| Related | 6ZRX |
| Descriptor | DMATS type aromatic prenyltransferase, TRYPTOPHAN, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | complex, abba-barrel fold, prenyltransferase, transferase |
| Biological source | Micromonospora olivasterospora |
| Total number of polymer chains | 2 |
| Total formula weight | 82284.49 |
| Authors | Ostertag, E.,Stehle, T.,Zocher, G. (deposition date: 2020-07-15, release date: 2020-12-09, Last modification date: 2024-01-31) |
| Primary citation | Ostertag, E.,Zheng, L.,Broger, K.,Stehle, T.,Li, S.M.,Zocher, G. Reprogramming Substrate and Catalytic Promiscuity of Tryptophan Prenyltransferases. J.Mol.Biol., 433:166726-166726, 2020 Cited by PubMed Abstract: Prenylation is a process widely prevalent in primary and secondary metabolism, contributing to functionality and chemical diversity in natural systems. Due to their high regio- and chemoselectivities, prenyltransferases are also valuable tools for creation of new compounds by chemoenzymatic synthesis and synthetic biology. Over the last ten years, biochemical and structural investigations shed light on the mechanism and key residues that control the catalytic process, but to date crucial information on how certain prenyltransferases control regioselectivity and chemoselectivity is still lacking. Here, we advance a general understanding of the enzyme family by contributing the first structure of a tryptophan C5-prenyltransferase 5-DMATS. Additinally, the structure of a bacterial tryptophan C6-prenyltransferase 6-DMATS was solved. Analysis and comparison of both substrate-bound complexes led to the identification of key residues for catalysis. Next, site-directed mutagenesis was successfully implemented to not only modify the prenyl donor specificity but also to redirect the prenylation, thereby switching the regioselectivity of 6-DMATS to that of 5-DMATS. The general strategy of structure-guided protein engineering should be applicable to other related prenyltransferases, thus enabling the production of novel prenylated compounds. PubMed: 33249189DOI: 10.1016/j.jmb.2020.11.025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.652 Å) |
Structure validation
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