3EL6

Crystal Structure of the Erythromycin Dehydratase

3EL6 の概要

• エントリーDOI: 10.2210/pdb3el6/pdb
• 関連するPDBエントリー: 2FR0 2HG4
• 分子名称: Erythromycin dehydratase, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: dehydratase double hotdog fold cis-proline, acyltransferase, antibiotic biosynthesis, multifunctional enzyme, nadp, phosphopantetheine, transferase, lyase
• 由来する生物種: Saccharopolyspora erythraea
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32848.90

構造登録者

Keatinge-Clay, A.T. (登録日: 2008-09-20, 公開日: 2008-11-11, 最終更新日: 2024-04-03)

主引用文献

Keatinge-Clay, A.
Crystal structure of the erythromycin polyketide synthase dehydratase.
J.Mol.Biol., 384:941-953, 2008

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: 18952099
DOI: 10.1016/j.jmb.2008.09.084

実験手法

X-RAY DIFFRACTION (1.85 Å)