4LHE

Crystal structure of closed form of Monoacylglycerol Lipase

4LHE の概要

• エントリーDOI: 10.2210/pdb4lhe/pdb
• 分子名称: Thermostable monoacylglycerol lipase, CHLORIDE ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta hydrolase fold, hydrolase
• 由来する生物種: Bacillus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55041.50

構造登録者

Tsurumura, T.,Tsuge, H. (登録日: 2013-07-01, 公開日: 2014-07-02, 最終更新日: 2023-11-08)

主引用文献

Tsurumura, T.,Tsuge, H.
Substrate selectivity of bacterial monoacylglycerol lipase based on crystal structure
J.Struct.Funct.Genom., 15:83-89, 2014

PubMed Abstract: Lipases, which are conserved from bacteria to mammals, catalyze the hydrolysis of acylglycerol to free fatty acids and glycerol. Monoacylglycerol lipase (MGL) specifically catalyzes the hydrolysis of monoacylglycerol. Although there have been numerous studies of the structure of lipases, there have been few studies of MGL. Here, we report the crystal structure of authentic MGL isolated from Bacillus sp. H257 (bMGL). The crystal diffracts to 1.96 Å resolution. It belongs to space group P21212, and the unit cell parameters are a=99.7 Å, b=106.1 Å and c=43.0 Å. As in other lipases, three structural features for lipase activity are conserved in bMGL: the glycine-X-serine-X-glycine motif, catalytic triad and cap region. The structure of bMGL appears to be closed, as the cap region covers the active site entrance. The isolated bMGL hydrolyzed 2-AG, a known human MGL-specific substrate. Based on a 2-AG bound model, we discuss the substrate selectivity. The functional and structural features of bMGL provide insight how its substrate selectivity is determined and how specific inhibitors of bacterial MGL could be designed, which may be useful for development of novel antibiotics.

PubMed: 24894647
DOI: 10.1007/s10969-014-9181-2

実験手法

X-RAY DIFFRACTION (1.962 Å)