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首页> 外文期刊>The FEBS journal >Structural and functional investigation of the Small Ribosomal Subunit Biogenesis GTPase A (RsgA) from Pseudomonas aeruginosa
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Structural and functional investigation of the Small Ribosomal Subunit Biogenesis GTPase A (RsgA) from Pseudomonas aeruginosa

机译：来自假单胞菌铜绿假单胞菌的小核糖体亚基生物生成GTP酶A（RSGA）的结构和功能调查

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摘要

The Small Ribosomal Subunit Biogenesis GTPase A (RsgA) is a bacterial assembly factor involved in the late stages of the 30S subunit maturation. It is a multidomain GTPase in which the central circularly permutated GTPase domain is flanked by an OB domain and a Zn-binding domain. All three domains participate in the interaction with the 30S particle thus ensuring an efficient coupling between catalytic activity and biological function. In vivo studies suggested the relevance of rsgA in bacterial growth and cellular viability, but other pleiotropic roles of RsgA are also emerging. Here, we report the 3D structure of RsgA from Pseudomonas aeruginosa (PaRsgA) in the GDP-bound form. We also report a biophysical and biochemical characterization of the protein in both the GDP-bound and its nucleotide-free form. In particular, we report a kinetic analysis of the RsgA binding to GTP and GDP. We found that PaRsgA is able to bind both nucleotides with submicromolar affinity. The higher affinity towards GDP (K-D = 0.011 mu m) with respect to GTP (K-D = 0.16 mu m) is mainly ascribed to a smaller GDP dissociation rate. Our results confirm that PaRsgA, like most other GTPases, has a weak intrinsic enzymatic activity (k(CAT) = 0.058 min(-1)). Finally, the biological role of RsgA in P. aeruginosa was investigated, allowing us to conclude that rsgA is dispensable for P. aeruginosa growth but important for drug resistance and virulence in an animal infection model. Databases Coordinates and structure factors for the protein structure described in this manuscript have been deposited in the Protein Data Bank () with the accession code .
机译：小核糖体亚基生物生成GTP酶A（RSGA）是涉及30S亚单位成熟的晚期阶段的细菌组装因子。它是一种多麦田GTP酶，其中中心圆形置换的GTP酶结构域侧翼由OB结构域和Zn结合结构域侧翼。所有三个结构域都参与与30S颗粒的相互作用，从而确保催化活性和生物学功能之间有效耦合。在体内研究表明RSGA在细菌生长和细胞活力方面的相关性，但RSGA的其他型胸腺作用也是出现的。在这里，我们在GDP绑定形式中向Pseudomonas铜绿假单胞菌（Parsga）报告RSGA的3D结构。我们还报告了GDP结合及其核苷酸形式中蛋白质的生物物理和生化表征。特别是，我们报告了对GTP和GDP的RSGA结合的动力学分析。我们发现Parsga能够将两个核苷酸与亚微粒剂亲和力结合。对GDP（K-D =0.011μm）相对于GTP（K-D =0.16μm）的较高亲和力主要归因于较小的GDP解离速率。我们的结果证实，与大多数其他GTP酶一样，Parsga具有弱的内在酶活性（K（猫）= 0.058分钟（-1））。最后，研究了rsga在p.铜绿假单胞菌中的生物学作用，使我们得出结论，rsga可分配p.铜绿假单胞菌生长，但在动物感染模型中的耐药性和毒力很重要。本手稿中描述的蛋白质结构的数据库坐标和结构因素已被沉积在蛋白质数据库（）中，并附上加入代码。

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