2FR1

The first ketoreductase of the erythromycin synthase (crystal form 2)

2FR1 の概要

• エントリーDOI: 10.2210/pdb2fr1/pdb
• 関連するPDBエントリー: 2FR0
• 分子名称: erythromycin synthase, EryAI, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: short chain dehydrogenase/reductase, oxidoreductase
• 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: 51823.54

構造登録者

Keatinge-Clay, A.T.,Stroud, R.M. (登録日: 2006-01-18, 公開日: 2006-04-04, 最終更新日: 2024-04-03)

主引用文献

Keatinge-Clay, A.T.,Stroud, R.M.
The Structure of a Ketoreductase Determines the Organization of the beta-Carbon Processing Enzymes of Modular Polyketide Synthases
Structure, 14:737-748, 2006

PubMed Abstract: The structure of the ketoreductase (KR) from the first module of the erythromycin synthase with NADPH bound was solved to 1.79 A resolution. The 51 kDa domain has two subdomains, each similar to a short-chain dehydrogenase/reductase (SDR) monomer. One subdomain has a truncated Rossmann fold and serves a purely structural role stabilizing the other subdomain, which catalyzes the reduction of the beta-carbonyl of a polyketide and possibly the epimerization of an alpha-substituent. The structure enabled us to define the domain boundaries of KR, the dehydratase (DH), and the enoylreductase (ER). It also constrains the three-dimensional organization of these domains within a module, revealing that KR does not make dimeric contacts across the 2-fold axis of the module. The quaternary structure elucidates how substrates are shuttled between the active sites of polyketide synthases (PKSs), as well as related fatty acid synthases (FASs), and suggests how domains can be swapped to make hybrid synthases that produce novel polyketides.

PubMed: 16564177
DOI: 10.1016/j.str.2006.01.009

実験手法

X-RAY DIFFRACTION (1.79 Å)