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首页> 外文期刊>Journal of Molecular Biology >Structure-based functional classification of hypothetical protein MTH538 from Methanobacterium thermoautotrophicum.
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Structure-based functional classification of hypothetical protein MTH538 from Methanobacterium thermoautotrophicum.

机译：热自养甲烷甲烷菌的假设蛋白MTH538的基于结构的功能分类。

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摘要

The structure of MTH538, a previously uncharacterized hypothetical protein from Methanobacterium thermoautotrophicum, has been determined by NMR spectroscopy. MTH538 is one of numerous structural genomics targets selected in a genome-wide survey of uncharacterized sequences from this organism. MTH538 is a so-called singleton, a sequence not closely related to any other (known) sequences. The structure of MTH538 closely resembles the known structures of receiver domains from two component response regulator systems, such as CheY, and is similar to the structures of flavodoxins and GTP-binding proteins. Tests on MTH538 for characteristic activities of CheY and flavodoxin were negative. MTH538 did not become phosphorylated in the presence of acetyl phosphate and Mg(2+), although it appeared to bind Mg(2+). MTH538 also did not bind flavin mononucleotide (FMN) or coenzyme F(420). Nevertheless, sequence and structure parallels between MTH538/CheY and two families of ATPase/phosphatase proteins suggest that MTH538 may have a role in a phosphorylation-independent two-component response regulator system. Copyright 2000 Academic Press.
机译：MTH538的结构已通过NMR光谱法确定，MTH538是以前自热嗜甲烷杆菌的未表征假想蛋白。 MTH538是从该生物体的未表征序列的全基因组调查中选择的众多结构基因组学靶标之一。 MTH538是所谓的单例，与任何其他（已知）序列都不紧密相关的序列。 MTH538的结构与来自两个成分响应调节系统（例如CheY）的受体域的已知结构非常相似，并且与黄素毒素和GTP结合蛋白的结构相似。对MTH538的CheY和黄酮毒素特性活性的测试为阴性。 MTH538在乙酰磷酸和Mg（2+）的存在下没有被磷酸化，尽管它似乎与Mg（2+）结合。 MTH538也没有结合黄素单核苷酸（FMN）或辅酶F（420）。然而，MTH538 / CheY与两个ATPase /磷酸酶蛋白家族之间的序列和结构相似性表明，MTH538可能在不依赖磷酸化的两组分应答调节剂系统中起作用。版权所有2000学术出版社。

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