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On the solution structure of the T4 sliding clamp (gp45)

机译：关于T4滑动夹具（gp45）的解决方案结构

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摘要

Examination by time-resolved fluorescence spectroscopy of the trimeric bacteriophage T4 clamp protein labeled across its three subunit interfaces with a fluorescence resonance energy transfer (FRET) pair indicates that the clamp exists in just one state in solution, with one open and two closed interfaces. This is in contrast to what is observed in the X-ray crystal structure. The population distribution of the trFRET distance is bimodal, giving 67% as 17 Angstrom and 33% as 42 A. This leads to the conclusion that gp45 exists in an asymmetric open state in solution. The further increase in the separation of the FRET pair in the presence of the clamp loader and ATP may be ascribed to either further opening of the open interface or the opening of a closed interface. The ramifications for replisome remodeling by this pathway are discussed.
机译：通过时间分辨荧光光谱法检查的三聚体噬菌体T4钳蛋白在其三个亚基界面上标记了荧光共振能量转移（FRET）对，表明该钳仅以一种状态存在于溶液中，具有一个开放和两个封闭的界面。这与在X射线晶体结构中观察到的相反。 trFRET距离的总体分布是双峰的，给出67％的17埃和33％的42A。这得出结论，gp45在溶液中以不对称开放态存在。在存在夹具装载器和ATP的情况下，FRET对的分离的进一步增加可归因于开放接口的进一步开放或封闭接口的开放。讨论了该途径对复制体重塑的影响。

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