6J0U

Crystal Structure of the acyltransferase domain from the third module of the ansamitocin polyketide synthase

6J0U の概要

• エントリーDOI: 10.2210/pdb6j0u/pdb
• 分子名称: Type 1 modular polyketide synthase, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: acyltransferase, methoxymalonyl-acp, polyketide, transferase
• 由来する生物種: Actinosynnema pretiosum subsp. auranticum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 197362.51

構造登録者

Zhang, F.,Zheng, J. (登録日: 2018-12-26, 公開日: 2019-12-18, 最終更新日: 2023-11-22)

主引用文献

Zhang, F.,Ji, H.,Ali, I.,Deng, Z.,Bai, L.,Zheng, J.
Structural and Biochemical Insight into the Recruitment of Acyl Carrier Protein-Linked Extender Units in Ansamitocin Biosynthesis.
Chembiochem, 21:1309-1314, 2020

PubMed Abstract: A few acyltransferase (AT) domains of modular polyketide synthases (PKSs) recruit acyl carrier protein (ACP)-linked extender units with unusual C2 substituents to confer functionalities that are not available in coenzyme A (CoA)-linked ones. In this study, an AT specific for methoxymalonyl (MOM)-ACP in the third module of the ansamitocin PKS was structurally and biochemically characterized. The AT uses a conserved tryptophan residue at the entrance of the substrate binding tunnel to discriminate between different carriers. A W275R mutation switches its carrier specificity from the ACP to the CoA molecule. The acyl-AT complex structures clearly show that the MOM-ACP accepted by the AT has the 2S instead of the opposite 2R stereochemistry that is predicted according to the biosynthetic derivation from a d-glycolytic intermediate. Together, these results reveal the structural basis of ATs recognizing ACP-linked extender units in polyketide biosynthesis.

PubMed: 31777147
DOI: 10.1002/cbic.201900628

実験手法

X-RAY DIFFRACTION (1.79 Å)