5MPT

Structure of the citrinin polyketide synthase CMeT domain

5MPT の概要

• エントリーDOI: 10.2210/pdb5mpt/pdb
• 分子名称: Citrinin polyketide synthase, S-ADENOSYL-L-HOMOCYSTEINE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: pks, polyketide, natural product, domain deconstruction, citrinin, c-methylation, methyltransferase, transferase
• 由来する生物種: Monascus purpureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47268.19

構造登録者

Herbst, D.A.,Storm, P.A.,Townsend, C.A.,Maier, T. (登録日: 2016-12-19, 公開日: 2017-02-22, 最終更新日: 2025-12-10)

主引用文献

Storm, P.A.,Herbst, D.A.,Maier, T.,Townsend, C.A.
Functional and Structural Analysis of Programmed C-Methylation in the Biosynthesis of the Fungal Polyketide Citrinin.
Cell Chem Biol, 24:316-325, 2017

PubMed Abstract: Fungal polyketide synthases (PKSs) are large, multidomain enzymes that biosynthesize a wide range of natural products. A hallmark of these megasynthases is the iterative use of catalytic domains to extend and modify a series of enzyme-bound intermediates. A subset of these iterative PKSs (iPKSs) contains a C-methyltransferase (CMeT) domain that adds one or more S-adenosylmethionine (SAM)-derived methyl groups to the carbon framework. Neither the basis by which only specific positions on the growing intermediate are methylated ("programming") nor the mechanism of methylation are well understood. Domain dissection and reconstitution of PksCT, the fungal non-reducing PKS (NR-PKS) responsible for the first isolable intermediate in citrinin biosynthesis, demonstrates the role of CMeT-catalyzed methylation in precursor elongation and pentaketide formation. The crystal structure of the S-adenosyl-homocysteine (SAH) coproduct-bound PksCT CMeT domain reveals a two-subdomain organization with a novel N-terminal subdomain characteristic of PKS CMeT domains and provides insights into co-factor and ligand recognition.

PubMed: 28238725
DOI: 10.1016/j.chembiol.2017.01.008

実験手法

X-RAY DIFFRACTION (1.648 Å)