Premium
Co‐expression with chaperones can affect protein 3D structure as exemplified by loss‐of‐function variants of human prolidase
Author(s) -
Wątor Elżbieta,
Rutkiewicz Maria,
Weiss Manfred S.,
Wilk Piotr
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13877
Subject(s) - chemistry , protein data bank , cleavage (geology) , enzyme , biochemistry , protein structure , in vivo , heat shock protein , mutant , microbiology and biotechnology , biology , genetics , gene , paleontology , fracture (geology)
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.