Structural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1
| Autor: | Xenia Bogdanović, Johanna Schwenteit, Winfried Hinrichs, Gottfried J. Palm, B K Gudmundsdóttir, Rajesh K. Singh |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Protein Folding medicine.medical_treatment Biophysics Aeromonas salmonicida Biochemistry 03 medical and health sciences Bacterial Proteins Structural Biology Catalytic Domain Genetics medicine Protein precursor Molecular Biology Alanine Protease 030102 biochemistry & molecular biology biology Metalloendopeptidases Cell Biology biology.organism_classification Endopeptidase 030104 developmental biology Chaperone (protein) biology.protein Metalloendopeptidase Protein folding Protein Binding |
| Zdroj: | FEBS Letters. 590:3280-3294 |
| ISSN: | 0014-5793 |
| DOI: | 10.1002/1873-3468.12356 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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