7S6B

Crystal structure of modular polyketide synthase apo-Lsd14 from the Lasalocid biosynthesis pathway, trapped in the transacylation step

7S6B の概要

• エントリーDOI: 10.2210/pdb7s6b/pdb
• 分子名称: Polyketide synthase, ... (4 entities in total)
• 機能のキーワード: modular polyketide synthase, ketosynthase, acyltransferase, acyl carrier protein, biosynthetic protein
• 由来する生物種: Streptomyces lasalocidi; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 332236.98

構造登録者

Bagde, S.R.,Mathews, I.I.,Kim, C.-Y. (登録日: 2021-09-13, 公開日: 2021-11-03, 最終更新日: 2024-05-22)

主引用文献

Bagde, S.R.,Mathews, I.I.,Fromme, J.C.,Kim, C.Y.
Modular polyketide synthase contains two reaction chambers that operate asynchronously.
Science, 374:723-729, 2021

PubMed Abstract: Type I modular polyketide synthases are homodimeric multidomain assembly line enzymes that synthesize a variety of polyketide natural products by performing polyketide chain extension and β-keto group modification reactions. We determined the 2.4-angstrom-resolution x-ray crystal structure and the 3.1-angstrom-resolution cryo–electron microscopy structure of the Lsd14 polyketide synthase, stalled at the transacylation and condensation steps, respectively. These structures revealed how the constituent domains are positioned relative to each other, how they rearrange depending on the step in the reaction cycle, and the specific interactions formed between the domains. Like the evolutionarily related mammalian fatty acid synthase, Lsd14 contains two reaction chambers, but only one chamber in Lsd14 has the full complement of catalytic domains, indicating that only one chamber produces the polyketide product at any given time.

PubMed: 34735234
DOI: 10.1126/science.abi8532

実験手法

X-RAY DIFFRACTION (2.35 Å)