Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-83

Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-83 Descriptor: 3-hydroxyacyl-CoA dehydrogenase, 4-phenylbenzenesulfonic acid, GLYCEROL, ... Authors: Dalwani, S, Wierenga, R.K, Venkatesan, R. Deposit date: 2023-04-12 Release date: 2024-01-24 Last modified: 2024-08-14 Method: X-RAY DIFFRACTION (2.33 Å) Cite: Crystallographic fragment-binding studies of the Mycobacterium tuberculosis trifunctional enzyme suggest binding pockets for the tails of the acyl-CoA substrates at its active sites and a potential substrate-channeling path between them. Acta Crystallogr D Struct Biol, 80, 2024与片段M-83结合的结核分枝杆菌（Mycobacterium tuberculosis）β-氧化三功能酶的结构 描述项：3-羟酰基辅酶A脱氢酶（3-hydroxyacyl-CoA dehydrogenase）、4-苯基苯磺酸、甘油（GLYCEROL）等 作者：Dalwani S、Wierenga R.K、Venkatesan R 存储日期：2023-04-12 发布日期：2024-01-24 最后修改日期：2024-08-14 实验方法：X射线衍射（X-RAY DIFFRACTION），分辨率2.33埃（Å） 引用说明：针对结核分枝杆菌三功能酶的晶体学片段结合研究表明，其活性位点存在酰基辅酶A底物尾部的结合口袋，且二者之间存在潜在的底物通道路径。该成果发表于《Acta Crystallogr D Struct Biol》2024年，第80卷。