6Q4S
Crystal structure of a-eudesmol synthase
Summary for 6Q4S
| Entry DOI | 10.2210/pdb6q4s/pdb |
| Descriptor | Pentalenene synthase, CHLORIDE ION (3 entities in total) |
| Functional Keywords | sesquiterpene, terpene synthase, plant protein, unknown function |
| Biological source | Streptomyces chartreusis NRRL 3882 |
| Total number of polymer chains | 1 |
| Total formula weight | 39534.18 |
| Authors | Correia Cordeiro, R.S.,Hakansson, M.,Logan, D.T.,Kourist, R. (deposition date: 2018-12-06, release date: 2018-12-19, Last modification date: 2024-01-24) |
| Primary citation | Kracht, O.N.,Correia Cordeiro, R.S.,Hakansson, M.,Stockmann, J.,Sander, D.,Bandow, J.,Senges, C.H.R.,Logan, D.T.,Kourist, R. Discovery of three novel sesquiterpene synthases from Streptomyces chartreusis NRRL 3882 and crystal structure of an alpha-eudesmol synthase. J.Biotechnol., 297:71-77, 2019 Cited by PubMed Abstract: With more than 50,000 members, terpenoids are one of the most important classes of natural products and show an enormous diversity. Due to their unique odors and specific bioactivities they already find wide application in the flavor, fragrance and pharma industries. Since most terpenoids can only be obtained by natural product extraction, the discovery of biosynthetic genes for the generation of terpene diversity becomes increasingly important. This study describes the discovery of three novel sesquiterpene synthases from Streptomyces chartreusis with preference for the formation of germacradiene-11-ol, α-eudesmol and α-amorphene respectively. The α-eudesmol synthase showed formation of 10-epi-δ-eudesmol and elemol as side products. Eudesmol-isomers are known to have repellent activity, which makes this enzyme a potential catalyst for products for the prevention of mosquito-related disease. The determination of the structure of the apo-enzyme of α-eudesmol synthase from S. chartreusis provides the first structural insights into an eudesmol-forming enzyme. PubMed: 30928538DOI: 10.1016/j.jbiotec.2019.03.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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