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Structural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1

TitleStructural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1
Publication TypeJournal Article
Year of Publication2016
AuthorsBogdanovi, X, Palm, GJ, Schwenteit, J, Singh, RK, Gudmundsdottir, BK, Hinrichs, W
JournalFEBS Letters
Issue590
Pagination3280–3294
Abstract

The Gram-negative bacterium Aeromonas salmonicida is a fish pathogen for various fish species worldwide. Aeromonas salmonicida subsp. Achromogenes produces the extracellular, toxic zinc endopeptidase AsaP1. Crystal structure analyses at 2.0 A resolution of two proteolytically inactive AsaP1 variants show the polypeptide folding of the protease domain and the propeptide domain. These first crystal structure analyses of a precursor of a deuterolysin-like aspzincin protease provide insights into propeptide function, and specific substrate binding. A lysine side chain of the propeptide binds in the hydrophobic S1’-pocket interacting with three carboxylate side chains. An AsaP1 variant with a lysine to alanine exchange identifies the chaperone function of the propeptide.

DOI10.1002/1873-3468.12356
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