Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa.
Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa.
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DOI：
10.1371/journal.pone.0063161
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
Schneider G
中科院分区：
文献类型：
--
作者：
Jacewicz A;Izumi A;Brunner K;Schnell R;Schneider G
3-聚异戊二烯基-4-羟基苯甲酸酯脱羧酶（UbiD）在泛醌的生物合成中催化3-聚异戊二烯基-4-羟基苯甲酸酯转化为2-聚异戊二烯基苯酚。铜绿假单胞菌含有两个基因（PA 0254和PA 5237），它们在序列上与推定的UbiD酶相关。生物信息学分析表明，UbiD序列家族可分为两个亚类，PA 5237和PA 0254属于该家族的不同分支。用单波长反常衍射和分子置换法测定了PA 0254的三维结构，其分辨率分别为1.95和2.3 μ m。PA 0254的亚基由三个结构域组成，N-末端α/β结构域，具有黄素还原酶家族相似折叠的分裂β桶和具有UbiD蛋白家族拓扑特征的C-末端α/β结构域。中间结构域含有一个金属结合位点，邻近一个大的开放裂缝，可能代表活性位点。结合镁离子的两种蛋白配体His 188和Glu 229在PA 0254亚类中不变，在来自分裂β-桶折叠家族的FMN结合蛋白中的一种中发现的相应金属位点中也是保守的。PA 0254形成的六聚体UbiD与E.大肠杆菌和铜绿假单胞菌，同源二聚体。在PA 0254型酶的环区域中插入四个残基导致与六聚体组装不相容的结构差异。
The 3-polyprenyl-4-hydroxybenzoate decarboxylase (UbiD) catalyzes the conversion of 3-polyprenyl-4-hydroxybenzoate to 2-polyprenylphenol in the biosynthesis of ubiquinone. Pseudomonas aeruginosa contains two genes (PA0254 and PA5237) that are related in sequence to putative UbiD enzymes. A bioinformatics analysis suggests that the UbiD sequence family can be divided into two subclasses, with PA5237 and PA0254 belonging to different branches of this family. The three-dimensional structure of PA0254 has been determined using single wavelength anomalous diffraction and molecular replacement in two different crystal forms to resolutions of 1.95 and 2.3 Å, respectively. The subunit of PA0254 consists of three domains, an N-terminal α/β domain, a split β-barrel with a similar fold of a family of flavin reductases and a C-terminal α/β domain with a topology characteristic for the UbiD protein family. The middle domain contains a metal binding site adjacent to a large open cleft that may represent the active site. The two protein ligands binding a magnesium ion, His188 and Glu229, invariant in the PA0254 subclass, are also conserved in a corresponding metal site found in one of the FMN binding proteins from the split β-barrel fold family. PA0254 forms, in contrast to the hexameric UbiD from E. coli and P. aeruginosa, a homo-dimer. Insertion of four residues in a loop region in the PA0254 type enzymes results in structural differences that are incompatible with hexamer assembly.
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影响因子：
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作者：
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影响因子：
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作者：
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通讯作者：
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