6EIC

Crystal structure of Rv0183, a Monoglyceride Lipase from Mycobacterium Tuberculosis

6EIC の概要

• エントリーDOI: 10.2210/pdb6eic/pdb
• 分子名称: Mycobacterium Tuberculosis Monoglyceride Lipase, SULFATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
• 機能のキーワード: monoglycerid lipase, hydrolase, lipase, alpha/beta hydrolase
• 由来する生物種: Mycobacterium tuberculosis H37Rv
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 91408.19

構造登録者

Aschauer, P.,Pavkov-Keller, T.,Oberer, M. (登録日: 2017-09-19, 公開日: 2018-06-27, 最終更新日: 2024-06-19)

主引用文献

Aschauer, P.,Zimmermann, R.,Breinbauer, R.,Pavkov-Keller, T.,Oberer, M.
The crystal structure of monoacylglycerol lipase from M. tuberculosis reveals the basis for specific inhibition.
Sci Rep, 8:8948-8948, 2018

PubMed Abstract: Monoacylglycerol lipases (MGLs) are enzymes that hydrolyze monoacylglycerol into a free fatty acid and glycerol. Fatty acids can be used for triacylglycerol synthesis, as energy source, as building blocks for energy storage, and as precursor for membrane phospholipids. In Mycobacterium tuberculosis, fatty acids also serve as precursor for polyketide lipids like mycolic acids, major components of the cellular envelope associated to resistance for drug. We present the crystal structure of the MGL Rv0183 from Mycobacterium tuberculosis (mtbMGL) in open conformation. The structure reveals remarkable similarities with MGL from humans (hMGL) in both, the cap region and the α/β core. Nevertheless, mtbMGL could not be inhibited with JZL-184, a known inhibitor of hMGL. Docking studies provide an explanation why the activity of mtbMGL was not affected by the inhibitor. Our findings suggest that specific inhibition of mtbMGL from Mycobacterium tuberculosis, one of the oldest recognized pathogens, is possible without influencing hMGL.

PubMed: 29895832
DOI: 10.1038/s41598-018-27051-7

実験手法

X-RAY DIFFRACTION (1.8 Å)