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首页> 外文期刊>Journal of Physics. Condensed Matter >Large-scale structure of RecA protein from Deinococcus radiodurance and its complexes in solution
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Large-scale structure of RecA protein from Deinococcus radiodurance and its complexes in solution

机译：Deinococcus radiodurance的RecA蛋白的大规模结构及其溶液复合物

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摘要

Different conformational states of the filaments formed by RecA protein from a radiation resistant strain Deinococcus radiodurance (RecA(Dr)) in solution were investigated using small angle neutron scattering. Scattering by the protein self-polymer was consistent with a long helix model, with the pitch of the helix being lower than that in the crystal structure. Compared to those of RecA proteins from Escherichia coli and Pseudomonas aeruginosa, helical filaments of RecA from D. radiodurance exhibited a lower helical pitch and lower stability at low Mg2+ concentrations or under conditions of elevated ionic strength in the absence of ATP (adenosine triphosphate). Formation of an active filament upon binding of ATP gamma S and either single- or double-stranded DNA brought about a significant increase in the helix pitch and a moderate decrease in the cross-sectional gyration radius, but resulted in little change in the number of monomers per helix turn. The helix pitch value of the RecA(Dr) presynaptic complex was conservative and close to that found for other RecA proteins and their analogs.
机译：使用小角度中子散射研究了抗辐射菌株Deinococcus radiodurance（RecA（Dr））在溶液中由RecA蛋白形成的细丝的不同构象状态。蛋白质自聚物的散射与长螺旋模型一致，螺旋的节距低于晶体结构中的节距。与来自大肠杆菌和铜绿假单胞菌的RecA蛋白相比，来自放射线虫的RecA螺旋丝在低Mg2 +浓度下或在缺乏ATP（三磷酸腺苷）的离子强度条件下表现出较低的螺旋间距和较低的稳定性。 ATPγS与单链或双链DNA结合后形成活性丝，导致螺旋螺距显着增加，横截面回转半径适度降低，但丝束数目几乎没有变化。每螺旋转数的单体数。 RecA（Dr）突触前复合物的螺旋螺距值是保守的，接近于其他RecA蛋白及其类似物的螺距。

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