7F27

Crystal structure of polyketide ketosynthase

7F27 の概要

• エントリーDOI: 10.2210/pdb7f27/pdb
• 分子名称: 3-oxoacyl-(Acyl-carrier-protein) synthase (2 entities in total)
• 機能のキーワード: thiolase fold, ketosynthase, ligase
• 由来する生物種: Acinetobacter baumannii (strain ACICU)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 174990.98

構造登録者

Kim, Y.,Lee, W.C. (登録日: 2021-06-10, 公開日: 2022-06-15, 最終更新日: 2023-11-29)

主引用文献

Lee, W.C.,Choi, S.,Jang, A.,Yeon, J.,Hwang, E.,Kim, Y.
Structural basis of the complementary activity of two ketosynthases in aryl polyene biosynthesis.
Sci Rep, 11:16340-16340, 2021

PubMed Abstract: Aryl polyenes (APE) are one of the most widespread secondary metabolites among gram-negative bacteria. In Acinetobacter baumannii, strains belonging to the virulent global clone 2 (GC2) mostly contain APE biosynthesis genes; its relevance in elevated pathogenicity is of great interest. APE biosynthesis gene clusters harbor two ketosynthases (KSs): the heterodimeric KS-chain length factor complex, ApeO-ApeC, and the homodimeric ketoacyl-acyl carrier protein synthase I (FabB)-like KS, ApeR. The role of the two KSs in APE biosynthesis is unclear. We determined the crystal structures of the two KSs from a pathogenic A. baumannii strain. ApeO-ApeC and ApeR have similar cavity volumes; however, ApeR has a narrow cavity near the entrance. In vitro assay based on the absorption characteristics of polyene species indicated the generation of fully elongated polyene with only ApeO-ApeC, probably because of the funnel shaped active site cavity. However, adding ApeR to the reaction increases the throughput of APE biosynthesis. Mutagenesis at Tyr135 in the active site cavity of ApeR reduces the activity significantly, which suggests that the stacking of the aryl group between Tyr135 and Phe202 is important for substrate recognition. Therefore, the two KSs function complementarily in the generation of APE to enhance its production.

PubMed: 34381152
DOI: 10.1038/s41598-021-95890-y

実験手法

X-RAY DIFFRACTION (1.806 Å)