5GNE

Crystal structure of LapB from Legionella pneumophila

Summary for 5GNE

• Entry DOI: 10.2210/pdb5gne/pdb
• Descriptor: Leucine aminopeptidase, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: aminopeptidase, legionella pneumophila, pa domain, autoinhibition, hydrolase
• Biological source: Legionella pneumophila
• Total number of polymer chains: 2
• Total formula weight: 84960.39

Authors

Zhang, N.,Ge, H. (deposition date: 2016-07-20, release date: 2017-08-30, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)