4NAO
Crystal structure of EasH
Summary for 4NAO
| Entry DOI | 10.2210/pdb4nao/pdb |
| Related | 2A1X 2OPW |
| Descriptor | Putative oxygenase, HEXAETHYLENE GLYCOL, 2-OXOGLUTARIC ACID, ... (6 entities in total) |
| Functional Keywords | jelly-roll fold, fe binding, oxidoreductase |
| Biological source | Claviceps purpurea (Ergot fungus) |
| Total number of polymer chains | 1 |
| Total formula weight | 37396.00 |
| Authors | Janke, R.,Havemann, J.,Vogel, D.,Keller, U.,Loll, B. (deposition date: 2013-10-22, release date: 2014-01-15, Last modification date: 2024-02-28) |
| Primary citation | Havemann, J.,Vogel, D.,Loll, B.,Keller, U. Cyclolization of d-lysergic Acid alkaloid peptides. Chem.Biol., 21:146-155, 2014 Cited by PubMed Abstract: The tripeptide chains of the ergopeptines, a class of pharmacologically important D-lysergic acid alkaloid peptides, are arranged in a unique bicyclic cyclol based on an amino-terminal α-hydroxyamino acid and a terminal orthostructure. D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases LPS1 and LPS2 of the ergot fungus Claviceps purpurea and released as N-(D-lysergyl-aminoacyl)-lactams. We show total enzymatic synthesis of ergopeptines catalyzed by a Fe²⁺/2-ketoglutarate-dependent dioxygenase (EasH) in conjunction with LPS1/LPS2. Analysis of the reaction indicated that EasH introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at α-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group. Sequence analysis revealed that EasH belongs to the wide and diverse family of the phytanoyl coenzyme A hydroxylases. We provide a high-resolution crystal structure of EasH that is most similar to that of phytanoyl coenzyme A hydroxylase, PhyH, from human. PubMed: 24361048DOI: 10.1016/j.chembiol.2013.11.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.649 Å) |
Structure validation
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