5CZC

The structure of VinK

5CZC の概要

• エントリーDOI: 10.2210/pdb5czc/pdb
• 分子名称: Malonyl-CoA-[acyl-carrier-protein] transacylase, GLYCEROL, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: transferase, polyketide biosynthesis
• 由来する生物種: Streptomyces halstedii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72778.38

構造登録者

Miyanaga, A.,Iwasawa, S.,Shinohara, Y.,Kudo, F.,Eguchi, T. (登録日: 2015-07-31, 公開日: 2016-02-03, 最終更新日: 2024-03-20)

主引用文献

Miyanaga, A.,Iwasawa, S.,Shinohara, Y.,Kudo, F.,Eguchi, T.
Structure-based analysis of the molecular interactions between acyltransferase and acyl carrier protein in vicenistatin biosynthesis.
Proc.Natl.Acad.Sci.USA, 113:1802-1807, 2016

PubMed Abstract: Acyltransferases (ATs) are key determinants of building block specificity in polyketide biosynthesis. Despite the importance of protein-protein interactions between AT and acyl carrier protein (ACP) during the acyltransfer reaction, the mechanism of ACP recognition by AT is not understood in detail. Herein, we report the crystal structure of AT VinK, which transfers a dipeptide group between two ACPs, VinL and VinP1LdACP, in vicenistatin biosynthesis. The isolated VinK structure showed a unique substrate-binding pocket for the dipeptide group linked to ACP. To gain greater insight into the mechanism of ACP recognition, we attempted to crystallize the VinK-ACP complexes. Because transient enzyme-ACP complexes are difficult to crystallize, we developed a covalent cross-linking strategy using a bifunctional maleimide reagent to trap the VinK-ACP complexes, allowing the determination of the crystal structure of the VinK-VinL complex. In the complex structure, Arg-153, Met-206, and Arg-299 of VinK interact with the negatively charged helix II region of VinL. The VinK-VinL complex structure allows, to our knowledge, the first visualization of the interaction between AT and ACP and provides detailed mechanistic insights into ACP recognition by AT.

PubMed: 26831085
DOI: 10.1073/pnas.1520042113

実験手法

X-RAY DIFFRACTION (1.8 Å)