7S6C

CryoEM structure of modular PKS holo-Lsd14 stalled at the condensation step and bound to antibody fragment 1B2, composite structure

7S6C の概要

• エントリーDOI: 10.2210/pdb7s6c/pdb
• EMDBエントリー: 24862 24863 24864 24865 24866 24867 24868
• 分子名称: 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion, Fab 1B2 heavy chain, Fab 1B2 light chain, ... (5 entities in total)
• 機能のキーワード: modular polyketide synthase, ketosynthase, ketoreductase, acyl carrier protein, biosynthetic protein
• 由来する生物種: Saccharopolyspora erythraea; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 801535.35

構造登録者

Bagde, S.R.,Kim, C.-Y.,Fromme, J.C. (登録日: 2021-09-13, 公開日: 2021-11-03, 最終更新日: 2021-11-17)

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

ELECTRON MICROSCOPY (3.1 Å)