2Z5L

The first ketoreductase of the tylosin PKS

2Z5L の概要

• エントリーDOI: 10.2210/pdb2z5l/pdb
• 分子名称: Tylactone synthase starter module and modules 1 & 2 (2 entities in total)
• 機能のキーワード: short-chain dehydrogenase/reductase, rossmann fold, polyketide synthase ketoreductase, transferase
• 由来する生物種: Streptomyces fradiae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53306.01

構造登録者

Keatinge-Clay, A.T.,Stroud, R.M. (登録日: 2007-07-14, 公開日: 2007-08-28, 最終更新日: 2023-11-01)

主引用文献

Keatinge-Clay, A.T.
A tylosin ketoreductase reveals how chirality is determined in polyketides
Chem.Biol., 14:898-908, 2007

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: 17719489
DOI: 10.1016/j.chembiol.2007.07.009

実験手法

X-RAY DIFFRACTION (1.95 Å)