Co-expression with chaperones can affect protein 3D structure as exemplified by loss-of-function variants of human prolidase
| Autor: | Manfred S. Weiss, Elżbieta Wątor, Piotr Wilk, Maria Rutkiewicz |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Dipeptidases
Mutant Biophysics Gene Expression Cleavage (embryo) Biochemistry 03 medical and health sciences Protein Domains Structural Biology Loss of Function Mutation Heat shock protein Genetics medicine Humans Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences Prolidase deficiency Chemistry C-terminus 030302 biochemistry & molecular biology Cell Biology computer.file_format medicine.disease Protein Data Bank Recombinant Proteins Enzyme Inhouse research on structure dynamics and function of matter Protein folding computer Molecular Chaperones |
| Popis: | Prolidase catalyzes the cleavage of dipeptides containing proline on their C terminus. The reduction in prolidase activity is the cause of a rare disease named 'Prolidase Deficiency'. Local structural disorder was indicated as one of the causes for diminished prolidase activity. Previous studies showed that heat shock proteins can partially recover prolidase activity in vivo. To analyze this mechanism of enzymatic activity rescue, we compared the crystal structures of selected prolidase mutants expressed in the absence and in the presence of chaperones. Our results confirm that protein chaperones facilitate the formation of more ordered structures by their substrate protein. These results also suggest that the protein expression system needs to be considered as an important parameter in structural studies. DATABASES: The reported crystal structures and their associated structure factor amplitudes were deposited in the Protein Data Bank under the accession codes 6SRE, 6SRF, and 6SRG, respectively. |
| Databáze: | OpenAIRE |
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