3SLK

Structure of ketoreductase and enoylreductase didomain from modular polyketide synthase

3SLK の概要

• エントリーDOI: 10.2210/pdb3slk/pdb
• 分子名称: Polyketide synthase extender module 2, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION (3 entities in total)
• 機能のキーワード: rossmann fold, nadph, oxidoreductase
• 由来する生物種: Saccharopolyspora spinosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 170118.98

構造登録者

Zheng, J.,Gay, D.C.,Keatinge-Clay, A.T. (登録日: 2011-06-24, 公開日: 2012-05-30, 最終更新日: 2024-02-28)

主引用文献

Zheng, J.,Gay, D.C.,Demeler, B.,White, M.A.,Keatinge-Clay, A.T.
Divergence of multimodular polyketide synthases revealed by a didomain structure.
Nat.Chem.Biol., 8:615-621, 2012

PubMed Abstract: The enoylreductase (ER) is the final common enzyme from modular polyketide synthases (PKSs) to be structurally characterized. The 3.0 Å-resolution structure of the didomain comprising the ketoreductase (KR) and ER from the second module of the spinosyn PKS reveals that ER shares an ∼600-Å(2) interface with KR distinct from that of the related mammalian fatty acid synthase (FAS). In contrast to the ER domains of the mammalian FAS, the ER domains of the second module of the spinosyn PKS do not make contact across the two-fold axis of the synthase. This monomeric organization may have been necessary in the evolution of multimodular PKSs to enable acyl carrier proteins to access each of their cognate enzymes. The isolated ER domain showed activity toward a substrate analog, enabling us to determine the contributions of its active site residues.

PubMed: 22634636
DOI: 10.1038/nchembio.964

実験手法

X-RAY DIFFRACTION (3 Å)