4U3V

Crystal structure of the trans-acyltransferase polyketide synthase enoyl-isomerase

4U3V の概要

• エントリーDOI: 10.2210/pdb4u3v/pdb
• 分子名称: Polyketide synthase PksR (2 entities in total)
• 機能のキーワード: isomerase, double-hotdog, polyketide, trans-at
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32662.00

構造登録者

Gay, D.C.,Spear, P.J.,Keatinge-Clay, A.T. (登録日: 2014-07-22, 公開日: 2014-08-20, 最終更新日: 2023-12-27)

主引用文献

Gay, D.C.,Spear, P.J.,Keatinge-Clay, A.T.
A Double-Hotdog with a New Trick: Structure and Mechanism of the trans-Acyltransferase Polyketide Synthase Enoyl-isomerase.
Acs Chem.Biol., 9:2374-2381, 2014

PubMed Abstract: Many polyketide natural products exhibit invaluable medicinal properties, yet much remains to be understood regarding the machinery responsible for their biosynthesis. The recently discovered trans-acyltransferase polyketide synthases employ processing enzymes that catalyze modifications unique from those of the classical cis-acyltransferase polyketide synthases. The enoyl-isomerase domains of these megasynthases shift double bonds and are well-represented by an enzyme that helps forge the triene system within the antibiotic produced by the prototypical bacillaene synthase. This first crystal structure of an enoyl-isomerase, at 1.73 Å resolution, not only revealed relationships between this class of enzymes and dehydratases but also guided an investigation into the mechanism of double bond migration. The catalytic histidine, positioned differently from that of dehydratases, was demonstrated to independently shuttle a proton between the γ- and α-positions of the intermediate. This unprecedented mechanism highlights the catalytic diversity of divergent enzymes within trans-acyltransferase polyketide synthases.

PubMed: 25089587
DOI: 10.1021/cb500459b

実験手法

X-RAY DIFFRACTION (1.73 Å)