5YO8
Crystal structure of beta-C25/C30/C35-prene synthase
Summary for 5YO8
| Entry DOI | 10.2210/pdb5yo8/pdb |
| Descriptor | Tetraprenyl-beta-curcumene synthase (2 entities in total) |
| Functional Keywords | terpene synthase, lyase |
| Biological source | Bacillus alcalophilus ATCC 27647 = CGMCC 1.3604 |
| Total number of polymer chains | 2 |
| Total formula weight | 83759.33 |
| Authors | Fujihashi, M.,Miki, K. (deposition date: 2017-10-27, release date: 2018-05-09, Last modification date: 2024-03-27) |
| Primary citation | Fujihashi, M.,Sato, T.,Tanaka, Y.,Yamamoto, D.,Nishi, T.,Ueda, D.,Murakami, M.,Yasuno, Y.,Sekihara, A.,Fuku, K.,Shinada, T.,Miki, K. Crystal structure and functional analysis of large-terpene synthases belonging to a newly found subclass. Chem Sci, 9:3754-3758, 2018 Cited by PubMed Abstract: Thousands of terpenes have been identified to date. However, only two classes of enzymes are known to be involved in their biosynthesis, and each class has characteristic amino-acid motifs. We recently identified a novel large-terpene (C/C/C) synthase, which shares no motifs with known enzymes. To elucidate the molecular mechanism of this enzyme, we determined the crystal structure of a large-β-prene synthase from (BalTS). Surprisingly, the overall structure of BalTS is similar to that of the α-domain of class I terpene synthases although their primary structures are totally different from each other. Two novel aspartate-rich motifs, DYLDNLxD and DY(F,L,W)IDxxED, are identified, and mutations of any one of the aspartates eliminate its enzymatic activity. The present work leads us to propose a new subclass of terpene synthases, class IB, which is probably responsible for large-terpene biosynthesis. PubMed: 29780507DOI: 10.1039/c8sc00289d PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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