2Z5L
The first ketoreductase of the tylosin PKS
Summary for 2Z5L
| Entry DOI | 10.2210/pdb2z5l/pdb |
| Descriptor | Tylactone synthase starter module and modules 1 & 2 (2 entities in total) |
| Functional Keywords | short-chain dehydrogenase/reductase, rossmann fold, polyketide synthase ketoreductase, transferase |
| Biological source | Streptomyces fradiae |
| Total number of polymer chains | 1 |
| Total formula weight | 53306.01 |
| Authors | Keatinge-Clay, A.T.,Stroud, R.M. (deposition date: 2007-07-14, release date: 2007-08-28, Last modification date: 2023-11-01) |
| Primary citation | Keatinge-Clay, A.T. A tylosin ketoreductase reveals how chirality is determined in polyketides Chem.Biol., 14:898-908, 2007 Cited by PubMed Abstract: Because it controls the majority of polyketide stereocenters, the ketoreductase (KR) is a central target in engineering polyketide synthases (PKSs). To elucidate the mechanisms of stereocontrol, the structure of KR from the first module of the tylosin PKS was determined. A comparison with a recently solved erythromycin KR that operates on the same substrate explains why their products have opposite alpha-substituent chiralities. The structure reveals how polyketides are guided into the active site by key residues in different KR types. There are four types of reductase-competent KRs, each capable of fixing a unique combination of alpha-substituent and beta-hydroxyl group chiralities, as well as two types of reductase-incompetent KRs that control alpha-substituent chirality alone. A protocol to assign how a module will enforce substituent chirality based on its sequence is presented. PubMed: 17719489DOI: 10.1016/j.chembiol.2007.07.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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