6SRF

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

6SRF の概要

• エントリーDOI: 10.2210/pdb6srf/pdb
• 分子名称: Xaa-Pro dipeptidase, MANGANESE (II) ION, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: dipeptidase, metallohydrolase, prolidase, pathological variants, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 109083.45

構造登録者

Wator, E.,Wilk, P. (登録日: 2019-09-05, 公開日: 2020-07-15, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.847 Å)