6l77

Publication Abstract from PubMed

MS5 is a meiosis-related protein belonging to the Brassicaceae-specific domain of unknown function family and characterized by the MS5 superfamily domain (MSD). In this study, we elucidated the three-dimensional crystal structure and potential biochemical function of the MSD. It was observed that the MSD adopts a cystatin-like fold, mainly consisting of a central alpha-helix and four- or five-stranded antiparallel beta-sheets that wrap around it. However, unlike cystatins, which inhibit cysteine proteases, the MSD displayed allosteric activation of papain. We believe that our study provides insight into novel mechanisms of proteolytic enzyme regulation and may serve as a basis for functional studies of the MS5 family proteins in plants.

Structural analysis of the meiosis-related protein MS5 reveals non-canonical papain enhancement by cystatin-like folds.,Wang X, Gao Y, Guan Z, Xie Z, Zhang D, Yin P, Yang G, Hong D, Xin Q FEBS Lett. 2020 Aug;594(15):2462-2471. doi: 10.1002/1873-3468.13817. Epub 2020, May 26. PMID:32415887^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.