Evolutionary Persistence of the Molybdopyranopterin-Containing Sulfite Oxidase Protein Fold
Evolutionary Persistence of the Molybdopyranopterin-Containing Sulfite Oxidase Protein Fold
复制标题
DOI：
10.1128/mmbr.00041-07
复制
发表时间：
2008-06
影响因子：
12.9
通讯作者：
Gregory J. Workun;Kamila Moquin;R. Rothery;J. Weiner
中科院分区：
文献类型：
--
作者：
Gregory J. Workun;Kamila Moquin;R. Rothery;J. Weiner
由于其缺乏和在整个进化过程中的持续存在而引起的衰弱和致命的人类疾病都说明了腺苷酸酶的重要性。在这里，我们表明，蛋白质折叠的亚硫酸盐氧化酶（SUOX倍）的结构域中含有dopyranopterin可以发现在所有三个领域的生活。序列数据和蛋白质结构比较（二级结构匹配）的分析表明，SUOX折叠被发现在酶，具有相当不同的大分子结构，包括一个或多个结构域，有时辅助亚基。这些概述如下：（i）含有N-末端细胞色素b5结构域和与C-末端二聚化结构域融合的SUOX折叠的动物SUOX;（ii）含有与C-末端二聚化结构域融合的SUOX折叠的植物SUOX;（iii）来自大肠杆菌的YedY蛋白，其仅包含SUOX折叠;（iv）来自Starkeya novella的亚硫酸盐脱氢酶，其含有SUOX折叠、二聚化结构域和另外的c型细胞色素亚基;和（v）植物型硝酸盐还原酶，以Pichia angusta的硝酸盐还原酶为例，其含有N-末端SUOX折叠、二聚化结构域、细胞色素b5结构域和C-末端结合NADH的含黄素腺嘌呤二核苷酸的结构域。我们使用含有SUOX折叠的蛋白质的一级序列来挖掘559个相关蛋白质的序列。这些序列的一个非冗余子集的同源性产生，并将所得的进化枝进行分类序列基序分析的上下文中可用的蛋白质结构。基于基序分析，分支，和结构域保守性，我们能够假设一个合理的路径SUOX折叠酶的进化。
SUMMARY The importance of molybdoenzymes is exemplified both by the debilitating and fatal human diseases caused by their deficiency and by their persistence throughout evolution. Here, we show that the protein fold of the molybdopyranopterin-containing domain of sulfite oxidase (the SUOX fold) can be found in all three domains of life. Analyses of sequence data and protein structure comparisons (secondary structure matching) show that the SUOX fold is found in enzymes that have quite distinct macromolecular architectures comprising one or more domains and sometimes subsidiary subunits. These are summarized as follows: (i) animal SUOXs that contain an N-terminal cytochrome b5 domain and an SUOX fold fused to a C-terminal dimerization domain; (ii) plant SUOX that contains an SUOX fold fused to a C-terminal dimerization domain; (iii) the YedY protein from Escherichia coli, which comprises only the SUOX fold; (iv) the sulfite dehydrogenase from Starkeya novella that contains the SUOX fold, a dimerization domain, and an additional c-type cytochrome subunit; and (v) the plant-type nitrate reductases, exemplified by that of Pichia angusta, that contain an N-terminal SUOX fold, a dimerization domain, a cytochrome b5 domain, and a C-terminal NADH binding flavin adenine dinucleotide-containing domain. We used the primary sequences of the proteins containing an SUOX fold to mine 559 sequences of related proteins. A phylogeny of a nonredundant subset of these sequences was generated, and the resultant clades were categorized by sequence motif analyses in the context of the available protein structures. Based on the motif analyses, cladistics, and domain conservations, we are able to postulate a plausible pathway of SUOX fold enzyme evolution.