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Structural analysis of the meiosis‐related protein MS5 reveals non‐canonical papain enhancement by cystatin‐like folds
Author(s) -
Wang Xiang,
Gao Yupeng,
Guan Zeyuan,
Xie Zhaoqi,
Zhang Delin,
Yin Ping,
Yang Guangsheng,
Hong Dengfeng,
Xin Qiang
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 - 10.1002/1873-3468.13817
Subject(s) - papain , proteases , cystatin , allosteric regulation , biochemistry , antiparallel (mathematics) , chemistry , protein structure , protein domain , biology , enzyme , cystatin c , gene , physics , quantum mechanics , renal function , magnetic field
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 α‐helix and four‐ or five‐stranded antiparallel β‐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.