Structural analysis of the meiosis‐related protein MS5 reveals non‐canonical papain enhancement by cystatin‐like folds
Structural analysis of the meiosis‐related protein MS5 reveals non‐canonical papain enhancement by cystatin‐like folds
复制标题
减数分裂相关蛋白 MS5 的结构分析揭示了胱抑素样折叠的非典型木瓜蛋白酶增强作用
DOI：
10.1002/1873-3468.13817
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发表时间：
2020
期刊：
影响因子：
3.5
通讯作者：
Qiang Xin
中科院分区：
文献类型：
--
作者：
Xiang Wang;Yupeng Gao;Zeyuan Guan;Zhaoqi Xie;Delin Zhang;Ping Yin;Guangsheng Yang;Dengfeng Hong;Qiang Xin
MS5是一种减数分裂相关蛋白，属于十字花科未知功能家族的特异结构域，以MS5超家族结构域（MSD）为特征。在这项研究中，我们阐明了MSD的三维晶体结构和潜在的生化功能。观察到MSD采用半胱抑素样折叠，主要由中心α -螺旋和围绕其的四或五股反平行β -片组成。然而，与抑制半胱氨酸蛋白酶的胱抑素不同，MSD显示出木瓜蛋白酶的变构激活。我们相信我们的研究为揭示蛋白水解酶调控的新机制提供了新的思路，并可能为植物中MS5家族蛋白的功能研究奠定基础。
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.