Structural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1.
FEBS Lett
; 590(18): 3280-94, 2016 09.
Article
in En
| MEDLINE
| ID: mdl-27528449
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 Å 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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Metalloendopeptidases
/
Protein Folding
Language:
En
Journal:
FEBS Lett
Year:
2016
Document type:
Article
Affiliation country:
Alemania