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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The structure of the genomic Bacillus subtilis dUTPase: novel features in the Phe-lid.
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The structure of the genomic Bacillus subtilis dUTPase: novel features in the Phe-lid.

机译：基因组的结构枯草芽孢杆菌Phe-lid dUTPase:小说的特征。

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摘要

dUTPases are a ubiquitous family of enzymes that are essential for all organisms and catalyse the breakdown of 2-deoxyuridine triphosphate (dUTP). In Bacillus subtilis there are two homotrimeric dUTPases: a genomic and a prophage form. Here, the structures of the genomic dUTPase and of its complex with the substrate analogue dUpNHpp and calcium are described, both at 1.85 A resolution. The overall fold resembles that of previously solved trimeric dUTPases. The C-terminus, which contains one of the conserved sequence motifs, is disordered in both structures. The crystal of the complex contains six independent protomers which accommodate six dUpNHpp molecules, with three triphosphates in the trans conformation and the other three in the active gauche conformation. The structure of the complex confirms the role of several key residues that are involved in ligand binding and the position of the catalytic water. Asp82, which has previously been proposed to act as a general base, points away from the active site. In the complex Ser64 reorients in order to hydrogen bond the phosphate chain of the substrate. A novel feature has been identified: the position in the sequence of the ;Phe-lid', which packs against the uracil moiety, is adjacent to motif III, whereas in all other dUTPase structures the lid is in a conserved position in motif V of the flexible C-terminal arm. This requires a reconsideration of some aspects of the accepted mechanism.
机译：dUTPases无处不在的家族的酶是必不可少的对于所有生物和催化三磷酸分解2-deoxyuridine (dUTP)。在枯草芽孢杆菌有两个homotrimericdUTPases:基因和前噬菌体形式。基因组的结构dUTPase和它的与底物模拟dUpNHpp和复杂1.85钙,在解决。整个折叠类似于以前解决了三聚物的dUTPases。包含一个保守序列的主题,无序结构。复杂的包含六个独立的原体容纳六dUpNHpp分子,有三个三磷酸腺苷在反式构象其他三个活跃的偏转构象。复杂的结构确认的角色几个关键残基参与配位绑定和催化水的位置。Asp82,此前提议采取行动一般基础,远离活跃点网站。氢键的磷酸盐链衬底。的序列中的位置;Phe-lid’,包对尿嘧啶基,是吗毗邻第三主题,而在其他dUTPase结构盖子是守恒的灵活的位置在主题V c端手臂。方面的接受机制。

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