Structural and biochemical analysis of the Obg GTP binding protein
Structural and biochemical analysis of the Obg GTP binding protein
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DOI：
10.1016/s0969-2126(02)00882-1
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发表时间：
2002-11-01
期刊：
影响因子：
5.7
通讯作者：
Lima, CD
中科院分区：
文献类型：
--
作者：
Buglino, J;Shen, V;Lima, CD
Obg核苷酸结合蛋白家族与应激反应、染色体分配、复制起始、菌丝发育和孢子形成有关。Obg蛋白是一大群GTP结合蛋白之一，从细菌到人类都是保守的。家族成员包含两个高度保守的结构域，一个c端GTP结合结构域和一个n端富含甘氨酸的结构域。枯草芽孢杆菌Obg的结构分析揭示了各自的结构域结构以及它们如何通过载子和核苷酸结合构型的c端GTPase结构域的假定开关元件耦合。细菌和人Obg蛋白的生化分析结合Obg活性视野内ppGpp核苷酸的结构观察表明ppGpp在枯草芽孢杆菌中调节Obg功能的潜在作用。
The Obg nucleotide binding protein family has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to man. Members of the family contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain. Structural analysis of Bacillus subtilis Obg revealed respective domain architectures and how they are coupled through the putative switch elements of the C-terminal GTPase domain in apo and nucleotide-bound configurations. Biochemical analysis of bacterial and human Obg proteins combined with the structural observation of the ppGpp nucleotide within the Obg active sight suggest a potential role for ppGpp modulation of Obg function in B. subtilis.