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首页> 外文期刊>EMBO Journal >Protonation-mediated structural flexibility in the F conjugation regulatory protein, TraM
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Protonation-mediated structural flexibility in the F conjugation regulatory protein, TraM

机译：Protonation-mediated结构的灵活性F结合监管蛋白质,有轨电车

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摘要

TraM is essential for F plasmid-mediated bacterial conjugation, where it binds to the plasmid DNA near the origin of transfer, and recognizes a component of the transmembrane DNA transfer complex, TraD. Here we report the 1.40 A crystal structure of the TraM core tetramer (TraM58-127). TraM58-127 is a compact eight-helical bundle, in which the N-terminal helices from each protomer interact to form a central, parallel four-stranded coiled-coil, whereas each C-terminal helix packs in an antiparallel arrangement around the outside of the structure. Four protonated glutamic acid residues (Glu88) are packed in a hydrogen-bonded arrangement within the central four-helix bundle. Mutational and biophysical analyses indicate that this protonated state is in equilibrium with a deprotonated tetrameric form characterized by a lower helical content at physiological pH and temperature. Comparison of TraM to its Glu88 mutants predicted to stabilize the helical structure suggests that the protonated state is the active form for binding TraD in conjugation.
机译：有轨电车F plasmid-mediated细菌至关重要结合,结合质粒DNA附近的起源传输和识别组件的跨膜DNA转移复杂的,传统的。有轨电车的结构核心四聚物(tram58 - 127)。tram58 - 127是一个紧凑的eight-helical包从每个原体的n端螺旋相互作用形成一个中央,平行四股卷曲螺旋,而每个在一个反平行的c端螺旋包在外部的结构安排。四个质子化了的谷氨酸残基(Glu88)包装在一个氢键的安排吗在中央四螺旋束。和生物物理分析表明这一点使质子化状态是在平衡deprotonated四聚物的形式特征较低的螺旋在生理pH值和内容温度。突变体预测稳定螺旋结构表明,质子化了的状态结合传统的活性形式的结合。

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