3EL6
Crystal Structure of the Erythromycin Dehydratase
Summary for 3EL6
| Entry DOI | 10.2210/pdb3el6/pdb |
| Related | 2FR0 2HG4 |
| Descriptor | Erythromycin dehydratase, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | dehydratase double hotdog fold cis-proline, acyltransferase, antibiotic biosynthesis, multifunctional enzyme, nadp, phosphopantetheine, transferase, lyase |
| Biological source | Saccharopolyspora erythraea |
| Total number of polymer chains | 1 |
| Total formula weight | 32848.90 |
| Authors | Keatinge-Clay, A.T. (deposition date: 2008-09-20, release date: 2008-11-11, Last modification date: 2024-04-03) |
| Primary citation | Keatinge-Clay, A. Crystal structure of the erythromycin polyketide synthase dehydratase. J.Mol.Biol., 384:941-953, 2008 Cited by PubMed Abstract: The dehydratases (DHs) of modular polyketide synthases (PKSs) catalyze dehydrations that occur frequently in the biosynthesis of complex polyketides, yet little is known about them structurally or mechanistically. Here, the structure of a DH domain, isolated from the fourth module of the erythromycin PKS, is presented at 1.85 A resolution. As with the DH of the highly related animalian fatty acid synthase, the DH monomer possesses a double-hotdog fold. Two symmetry mates within the crystal lattice make a contact that likely represents the DH dimerization interface within an intact PKS. Conserved hydrophobic residues on the DH surface indicate potential interfaces with two other PKS domains, the ketoreductase and the acyl carrier protein. Mutation of an invariant arginine at the hypothesized acyl carrier protein docking site in the context of the erythromycin PKS resulted in decreased production of the erythromycin precursor 6-deoxyerythronolide B. The structure elucidates how the alpha-hydrogen and beta-hydroxyl group of a polyketide substrate interact with the catalytic histidine and aspartic acid in the DH active site prior to dehydration. PubMed: 18952099DOI: 10.1016/j.jmb.2008.09.084 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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