5GW8

Crystal structure of a putative DAG-like lipase (MgMDL2) from Malassezia globosa

5GW8 の概要

• エントリーDOI: 10.2210/pdb5gw8/pdb
• 分子名称: Hypothetical secretory lipase (Family 3), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: dag-like lipase, n-linked glycosylation, hydrolase
• 由来する生物種: Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65577.01

構造登録者

Xu, J.,Xu, H.,Liu, J. (登録日: 2016-09-09, 公開日: 2017-09-27, 最終更新日: 2023-11-08)

主引用文献

Lan, D.,Xu, H.,Xu, J.,Dubin, G.,Liu, J.,Iqbal Khan, F.,Wang, Y.
Malassezia globosa MgMDL2 lipase: Crystal structure and rational modification of substrate specificity.
Biochem. Biophys. Res. Commun., 488:259-265, 2017

PubMed Abstract: Lipases play an important role in physiological metabolism and diseases, and also have multiple industrial applications. Rational modification of lipase specificity may increase the commercial utility of this group of enzymes, but is hindered by insufficient mechanistic understanding. Here, we report the 2.0 Å resolution crystal structure of a mono- and di-acylglycerols lipase from Malassezia globosa (MgMDL2). Interestingly, residues Phe278 and Glu282 were found to involve in substrate recognition because mutation on each residue led to convert MgMDL2 to a triacylglycerol (TAG) lipase. The Phe278Ala and Glu282Ala mutants also acquired ability to synthesize TAGs by esterification of glycerol and fatty acids. By in silicon analysis, steric hindrance of these residues seemed to be key factors for the altered substrate specificity. Our work may shed light on understanding the unique substrate selectivity mechanism of mono- and di-acylglycerols lipases, and provide a new insight for engineering biocatalysts with desired catalytic behaviors for biotechnological application.

PubMed: 28433636
DOI: 10.1016/j.bbrc.2017.04.103

実験手法

X-RAY DIFFRACTION (2 Å)