4RZM
Crystal structure of the Lsd19-lasalocid A complex
Summary for 4RZM
| Entry DOI | 10.2210/pdb4rzm/pdb |
| Related | 3RGA |
| Descriptor | Epoxide hydrolase LasB, Lasalocid A, GLYCEROL, ... (7 entities in total) |
| Functional Keywords | ntf2-like fold, epoxide-opening cyclic ether formation, isomerization, isomerase |
| Biological source | Streptomyces lasaliensis |
| Total number of polymer chains | 2 |
| Total formula weight | 62920.04 |
| Authors | Mathews, I.I.,Hotta, K.,Chen, X.,Kim, C.-Y. (deposition date: 2014-12-22, release date: 2015-01-21, Last modification date: 2023-09-20) |
| Primary citation | Wong, F.T.,Hotta, K.,Chen, X.,Fang, M.,Watanabe, K.,Kim, C.Y. Epoxide hydrolase-lasalocid a structure provides mechanistic insight into polyether natural product biosynthesis. J.Am.Chem.Soc., 137:86-89, 2015 Cited by PubMed Abstract: Biosynthesis of some polyether natural products involves a kinetically disfavored epoxide-opening cyclic ether formation, a reaction termed anti-Baldwin cyclization. One such example is the biosynthesis of lasalocid A, an ionophore antibiotic polyether. During lasalocid A biosynthesis, an epoxide hydrolase, Lsd19, converts the bisepoxy polyketide intermediate into the tetrahydrofuranyl-tetrahydropyran product. We report the crystal structure of Lsd19 in complex with lasalocid A. The structure unambiguously shows that the C-terminal domain of Lsd19 catalyzes the intriguing anti-Baldwin cyclization. We propose a general mechanism for epoxide selection by ionophore polyether epoxide hydrolases. PubMed: 25535803DOI: 10.1021/ja511374k PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.33 Å) |
Structure validation
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