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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of the catalytic phosphatase domain of MTMR8: implications for dimerization, membrane association and reversible oxidation
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Structure of the catalytic phosphatase domain of MTMR8: implications for dimerization, membrane association and reversible oxidation

机译：催化磷酸酶结构域的MTMR8:对二聚作用,膜协会和可逆的氧化

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摘要

Myotubularin-related proteins are a large family of phosphoinositide phosphatases; their activity, stability and subcellular localization are regulated by dimeric interactions with other members of the family. Here, the crystal structure of the phosphatase domain of MTMR8 is reported. Conformational deviation of the two loops that mediate interaction with the PH-GRAM domain suggests that the PH-GRAM domain interacts differently with the phosphatase domain of each MTMR member. The protein exists as a dimer with twofold symmetry, providing insight into a novel mode of dimerization mediated by the phosphatase domain. Structural comparison and mutation studies suggest that Lys255 of MTMR8 interacts with the substrate diacylglycerol moiety, similar to Lys333 of MTMR2, although the positions of these residues are different. The catalytic activity of the MTMR8 phosphatase domain is inhibited by oxidation and is reversibly reactivated by reduction, suggesting the presence of an oxidation-protective intermediate other than a disulfide bond owing to the absence of a cysteine within a disulfide-bond distance from Cys338.
机译：Myotubularin-related蛋白质是一个大家庭的磷酸肌醇磷酸酯酶;稳定和亚细胞定位由二聚的交互与其他家庭的成员。MTMR8磷酸酶结构域报道。循环与PH-GRAM协调交互域表明PH-GRAM域进行交互不同的磷酸酶域MTMR成员。两个对称,提供洞察一部小说模式二聚作用介导的磷酸酶域。研究表明,Lys255 MTMR8交互与底物甘油二酯基,相似Lys333 MTMR2,尽管的位置这些残留物是不同的。MTMR8磷酸酶域的活动被氧化,是可逆的重新激活的减少,表明存在oxidation-protective的中间比二硫键由于缺乏半胱氨酸的二硫键的距离Cys338。

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