6SRF

Crystal Structure of Human Prolidase G278N variant expressed in the presence of chaperones

Summary for 6SRF

• Entry DOI: 10.2210/pdb6srf/pdb
• Descriptor: Xaa-Pro dipeptidase, MANGANESE (II) ION, SODIUM ION, ... (7 entities in total)
• Functional Keywords: dipeptidase, metallohydrolase, prolidase, pathological variants, hydrolase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 109083.45

Authors

Wator, E.,Wilk, P. (deposition date: 2019-09-05, release date: 2020-07-15, Last modification date: 2024-11-06)

Primary citation

Wator, E.,Rutkiewicz, M.,Weiss, M.S.,Wilk, P.
Co-expression with chaperones can affect protein 3D structure as exemplified by loss-of-function variants of human prolidase.
Febs Lett., 594:3045-3056, 2020

PubMed Abstract: 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.

PubMed: 32598484
DOI: 10.1002/1873-3468.13877

Experimental method

X-RAY DIFFRACTION (1.847 Å)