5GNE

Crystal structure of LapB from Legionella pneumophila

5GNE の概要

• エントリーDOI: 10.2210/pdb5gne/pdb
• 分子名称: Leucine aminopeptidase, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: aminopeptidase, legionella pneumophila, pa domain, autoinhibition, hydrolase
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84960.39

構造登録者

Zhang, N.,Ge, H. (登録日: 2016-07-20, 公開日: 2017-08-30, 最終更新日: 2024-10-09)

主引用文献

Zhang, N.,Yin, S.,Zhang, W.,Gong, X.,Zhang, N.,Fang, K.,Ge, H.
Crystal Structure and Biochemical Characterization of an Aminopeptidase LapB from Legionella pneumophila.
J. Agric. Food Chem., 65:7569-7578, 2017

PubMed Abstract: Aminopeptidases are a group of exopeptidases that catalyze the removal of a wide range of N-terminal amino acid residues from peptides and proteins. They have many important commercial applications in the food industry. We determined the crystal structure of an aminopeptidase LapB from Legionella pneumophila. The overall structure reveals that the N-terminal protease-associated (PA) domain presents a new fold and shields the active site cavity of the conserved C-terminal peptidase domain. The steady-state kinetic analysis of LapB and the PA domain deletion mutant indicate that the PA domain inhibited enzyme activity of the peptidase domain. Interestingly, the activity of LapB was largely increased by various organic solvents such as ethanol, propanol, and methanol at the concentration of 60% (v/v). CD analysis provided evidence that organic solvents induce the PA domain conformational changes that eliminate the inhibition role. The unique properties indicate the application potential of LapB in the food processing industry.

PubMed: 28776986
DOI: 10.1021/acs.jafc.7b02849

実験手法

X-RAY DIFFRACTION (2.5 Å)