7Q4J

A thermostable lipase from Thermoanaerobacter thermohydrosulfuricus in complex a monoacylglycerol intermediate

7Q4J の概要

• エントリーDOI: 10.2210/pdb7q4j/pdb
• 関連するPDBエントリー: 7Q4H
• 分子名称: Serine aminopeptidase S33 domain-containing protein, STEARIC ACID, N-OCTANE, ... (10 entities in total)
• 機能のキーワード: alpha/beta hydrolase, hydrolase, thermostable, monoacylglycerol, lipase
• 由来する生物種: Thermoanaerobacter thermohydrosulfuricus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62134.02

構造登録者

Pinotsis, N.,Wilmanns, M. (登録日: 2021-10-31, 公開日: 2023-05-10, 最終更新日: 2024-05-22)

主引用文献

Pinotsis, N.,Kruger, A.,Tomas, N.,Chatziefthymiou, S.D.,Litz, C.,Mortensen, S.A.,Daffe, M.,Marrakchi, H.,Antranikian, G.,Wilmanns, M.
Discovery of a non-canonical prototype long-chain monoacylglycerol lipase through a structure-based endogenous reaction intermediate complex.
Nat Commun, 14:7649-7649, 2023

PubMed Abstract: The identification and characterization of enzyme function is largely lacking behind the rapidly increasing availability of large numbers of sequences and associated high-resolution structures. This is often hampered by lack of knowledge on in vivo relevant substrates. Here, we present a case study of a high-resolution structure of an unusual orphan lipase in complex with an endogenous C18 monoacylglycerol ester reaction intermediate from the expression host, which is insoluble under aqueous conditions and thus not accessible for studies in solution. The data allowed its functional characterization as a prototypic long-chain monoacylglycerol lipase, which uses a minimal lid domain to position the substrate through a hydrophobic tunnel directly to the enzyme's active site. Knowledge about the molecular details of the substrate binding site allowed us to modulate the enzymatic activity by adjusting protein/substrate interactions, demonstrating the potential of our findings for future biotechnology applications.

PubMed: 38012138
DOI: 10.1038/s41467-023-43354-4

実験手法

X-RAY DIFFRACTION (1.91 Å)