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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：MTMR8催化磷酸酶结构域的结构：对二聚，膜缔合和可逆氧化的影响

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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：肌管蛋白相关蛋白是磷酸肌醇磷酸酶的一大家族。它们的活性，稳定性和亚细胞定位受与该家族其他成员的二聚体相互作用调节。在此，报道了MTMR8的磷酸酶结构域的晶体结构。介导与PH-GRAM域相互作用的两个环的构象偏差表明，PH-GRAM域与每个MTMR成员的磷酸酶域的相互作用不同。该蛋白质以具有双重对称性的二聚体形式存在，提供了对由磷酸酶结构域介导的新型二聚化模式的见识。结构比较和突变研究表明，MTMR8的Lys255与底物二酰基甘油部分相互作用，类似于MTMR2的Lys333，尽管这些残基的位置不同。 MTMR8磷酸酶结构域的催化活性被氧化抑制，并被还原可逆地重新激活，这表明除二硫键外还存在氧化保护中间体，这是由于在距Cys338的二硫键距离内不存在半胱氨酸。

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