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首页> 外文期刊>Journal of structural and functional genomics >NMR structure of the N-terminal domain of the replication initiator protein DnaA
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NMR structure of the N-terminal domain of the replication initiator protein DnaA

机译：复制起始蛋白DnaA N端结构域的NMR结构

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摘要

DnaA is an essential component in the initiation of bacterial chromosomal replication. DnaA binds to a series of 9 base pair repeats leading to oligomerization, recruitment of the DnaBC helicase, and the assembly of the replication fork machinery. The structure of the N-terminal domain (residues 1–100) of DnaA from Mycoplasma genitalium was determined by NMR spectroscopy. The backbone r.m.s.d. for the first 86 residues was 0.6?±?0.2 ? based on 742 NOE, 50 hydrogen bond, 46 backbone angle, and 88 residual dipolar coupling restraints. Ultracentrifugation studies revealed that the domain is monomeric in solution. Features on the protein surface include a hydrophobic cleft flanked by several negative residues on one side, and positive residues on the other. A negatively charged ridge is present on the opposite face of the protein. These surfaces may be important sites of interaction with other proteins involved in the replication process. Together, the structure and NMR assignments should facilitate the design of new experiments to probe the protein–protein interactions essential for the initiation of DNA replication.
机译：DnaA是启动细菌染色体复制的重要组成部分。 DnaA与一系列9个碱基对的重复序列结合，导致寡聚化，DnaBC解旋酶的募集以及复制叉机制的组装。生殖器支原体的DnaA的N末端结构域（残基1–100）的结构通过NMR光谱法确定。骨干r.m.s.d.前86个残基的0.6？±？0.2？基于742个NOE，50个氢键，46个主链角和88个残留的偶极耦合约束。超速离心研究表明，该域在溶液中是单体的。蛋白质表面的特征是疏水性裂缝，其一侧有多个负残基，而另一侧有正残基。蛋白质的相反面上存在带负电的脊。这些表面可能是与复制过程中涉及的其他蛋白质相互作用的重要部位。在一起，结构和NMR分配应有助于设计新的实验，以探究DNA复制起始所必需的蛋白质间相互作用。

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