Diversification of quiescin sulfhydryl oxidase in a preserved framework for redox relay.
Diversification of quiescin sulfhydryl oxidase in a preserved framework for redox relay.
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DOI：
10.1186/1471-2148-13-70
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发表时间：
2013-03-19
影响因子：
3.4
通讯作者：
Fass D
中科院分区：
文献类型：
--
作者：
Limor-Waisberg K;Ben-Dor S;Fass D
酶家族 Quiescin 硫氢基氧化酶 (QSOX) 的定义是存在氨基末端硫氧还蛋白折叠 (Trx) 结构域和羧基末端 Erv 家族硫氢基氧化酶结构域。 QSOX 酶可产生二硫键并将其转移至底物蛋白，存在于包括后生动物和植物在内的多种真核物种中，但真菌中不存在。植物和动物 QSOX 的活性位点氨基酸序列和非催化结构域的含量不同。因此，问题出现了，Trx-Erv 融合是否在所有 QSOX 酶中具有相同的机制意义，以及共享特征是否将 QSOX 的功能域与这些域独立出现的其他情况区分开来。通过对 QSOX 系统发育的研究以及根据最近确定的三维结构对 QSOX 序列多样性进行分析，我们寻求深入了解这种多域氧化还原联盟的起源和演变。使用更新的 QSOX 酶集合来确认和细化属于不同真核门的 QSOX 的结构域组成和活性位点序列基序模式的差异。除了动物和植物 QSOX 酶的预期系统发育差异之外，基于单个氧化还原活性 QSOX 结构域的树显示出植物进化早期 Trx 结构域的特殊区别。将 QSOX 结构域与 QSOX 家族以外的 Trx 和 Erv 结构域进行比较，揭示了几个序列和结构特征，这些特征清楚地将 QSOX 与包含这些结构域中的任何一个的其他酶区分开来。值得注意的是，这些特征存在于不同门的 QSOX 中，定位于在模拟域间氧化还原通信的 QSOX 结构中观察到的 Trx 和 Erv 域之间的界面。先前在动物和寄生虫 QSOX 中发现的域间电子中继基础设施在 QSOX 家族中广泛存在，包括植物酶。我们得出的结论是，QSOX 催化结构域的保守三维框架适应了氧化还原活性半胱氨酸周围氨基酸残基的谱系特异性差异和旁系同源多样性。我们的研究结果表明，QSOX 酶的特征不仅在于存在两个定义域折叠，而且还在于促进协调活性的特征。
The enzyme family Quiescin Sulfhydryl Oxidase (QSOX) is defined by the presence of an amino-terminal thioredoxin-fold (Trx) domain and a carboxy-terminal Erv family sulfhydryl oxidase domain. QSOX enzymes, which generate disulfide bonds and transfer them to substrate proteins, are present in a wide variety of eukaryotic species including metazoans and plants, but are absent from fungi. Plant and animal QSOXs differ in their active-site amino acid sequences and content of non-catalytic domains. The question arises, therefore, whether the Trx-Erv fusion has the same mechanistic significance in all QSOX enzymes, and whether shared features distinguish the functional domains of QSOX from other instances in which these domains occur independently. Through a study of QSOX phylogeny and an analysis of QSOX sequence diversity in light of recently determined three-dimensional structures, we sought insight into the origin and evolution of this multi-domain redox alliance. An updated collection of QSOX enzymes was used to confirm and refine the differences in domain composition and active-site sequence motif patterns of QSOXs belonging to various eukaryotic phyla. Beyond the expected phylogenetic distinction of animal and plant QSOX enzymes, trees based on individual redox-active QSOX domains show a particular distinction of the Trx domain early in plant evolution. A comparison of QSOX domains with Trx and Erv domains from outside the QSOX family revealed several sequence and structural features that clearly differentiate QSOXs from other enzymes containing either of these domains. Notably, these features, present in QSOXs of various phyla, localize to the interface between the Trx and Erv domains observed in structures of QSOX that model interdomain redox communication. The infrastructure for interdomain electron relay, previously identified for animal and parasite QSOXs, is found broadly across the QSOX family, including the plant enzymes. We conclude that the conserved three-dimensional framework of the QSOX catalytic domains accommodates lineage-specific differences and paralog diversification in the amino acid residues surrounding the redox-active cysteines. Our findings indicate that QSOX enzymes are characterized not just by the presence of the two defining domain folds but also by features that promote coordinated activity.
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影响因子：
4.4
作者：
Selles, Benjamin;Jacquot, Jean-Pierre;Rouhier, Nicolas
通讯作者：
Rouhier, Nicolas
DOI：
10.1038/nsb740
发表时间：
2002-01-01
期刊：
NATURE STRUCTURAL BIOLOGY
影响因子：
--
作者：
Gross, E;Sevier, CS;Fass, D
通讯作者：
Fass, D
影响因子：
5.6
作者：
Jones, DT
通讯作者：
Jones, DT
影响因子：
14.9
作者：
Thompson, JD;Gibson, TJ;Higgins, DG
通讯作者：
Higgins, DG
影响因子：
4.1
作者：
Chakravarthi, Seerna;Jessop, Catherine E.;Bulleid, Neil J.
通讯作者：
Bulleid, Neil J.