4RV2

Crystal Structure of (3R)-hydroxyacyl-ACP dehydratase HadAB hetero-dimer from Mycobacterium smegmatis

4RV2 の概要

• エントリーDOI: 10.2210/pdb4rv2/pdb
• 分子名称: UPF0336 protein MSMEG_1340/MSMEI_1302, MaoC family protein, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hotdog fold, lyase
• 由来する生物種: Mycobacterium smegmatis str. MC2 155; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31460.38

構造登録者

Biswas, R.,Hazra, D.,Dutta, D.,Das, A.K. (登録日: 2014-11-24, 公開日: 2015-02-11, 最終更新日: 2024-02-28)

主引用文献

Biswas, R.,Dutta, A.,Dutta, D.,Hazra, D.,Banerjee, D.R.,Basak, A.,Das, A.K.
Crystal structure of dehydratase component HadAB complex of mycobacterial FAS-II pathway.
Biochem.Biophys.Res.Commun., 458:369-374, 2015

PubMed Abstract: Fatty acid biosynthesis type II in mycobacteria delivers the fatty acids required for mycolic acid synthesis. The pathway employs a unique maoC like β-hydroxyacyl-ACP dehydratase HadAB or HadBC heterodimer in the third step of the elongation cycle. Here we report the crystal structure of the HadAB complex determined using a Pb-SIRAS method. Crystal structure aided with enzymatic study establishes the roles of HadA as a scaffolding component and HadB as a catalytic component together indispensable for the activity. The detailed structural analysis of HadAB in combination with MD simulation endorses the spatial orientation of the central hot-dog helix and the dynamic nature of its associated loop in regulation of substrate specificities in dehydratase/hydratase family enzymes.

PubMed: 25656575
DOI: 10.1016/j.bbrc.2015.01.119

実験手法

X-RAY DIFFRACTION (2.7 Å)