7VT1

Acyltransferase from the 9th Module of Salinomycin Polyketide Synthase

7VT1 の概要

• エントリーDOI: 10.2210/pdb7vt1/pdb
• 分子名称: Type I modular polyketide synthase (2 entities in total)
• 機能のキーワード: acyl transferase, transferase
• 由来する生物種: Streptomyces albus subsp. albus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97146.89

構造登録者

Feng, Y.,Zhang, F.,Zheng, J. (登録日: 2021-10-27, 公開日: 2022-06-08, 最終更新日: 2023-11-29)

主引用文献

Feng, Y.,Zhang, F.,Huang, S.,Deng, Z.,Bai, L.,Zheng, J.
Structural visualization of transient interactions between the cis-acting acyltransferase and acyl carrier protein of the salinomycin modular polyketide synthase.
Acta Crystallogr D Struct Biol, 78:779-791, 2022

PubMed Abstract: Transient protein-protein interactions between cis-acting acyltransferase (AT) and acyl carrier protein (ACP) domains are critical for the catalysis and processivity of modular polyketide synthases (mPKSs), but are challenging for structural characterization due to the intrinsically weak binding affinity. Here, a stable complex of cis-acting AT and ACP domains from the ninth module of the salinomycin mPKS was obtained using a maleimide cross-linker and the structure of the complex was determined at 2.6 Å resolution. The crystal structure shows that the AT in combination with the ketosynthase (KS)-to-AT linker forms a C-shaped architecture to embrace the ACP. The large hydrolase subdomain of the AT serves as a major binding platform for the ACP, while the small ferredoxin-like subdomain of the AT and the KS-to-AT linker cooperate with each other to constrain binding of the ACP. The importance of interface residues in cis-acting AT-ACP interactions was confirmed by mutagenesis assays. The interaction mode observed in the cis-acting AT-ACP complex is completely different from those observed in trans-acting AT-ACP complexes, where the ACP primarily contacts the small domain of the AT. The complex structure provides detailed mechanistic insights into AT-ACP recognition in cis-AT mPKSs.

PubMed: 35647924
DOI: 10.1107/S2059798322004612

実験手法

X-RAY DIFFRACTION (2.5 Å)