Conformational changes of a Swi2/Snf2 ATPase during its mechano-chemical cycle.
Conformational changes of a Swi2/Snf2 ATPase during its mechano-chemical cycle.
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DOI：
10.1093/nar/gkn040
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发表时间：
2008-04
影响因子：
14.9
通讯作者：
Michaelis J
中科院分区：
文献类型：
--
作者：
Lewis R;Dürr H;Hopfner KP;Michaelis J
蛋白质核酸界面的重塑是一项重要的生物学任务，通常由核酸刺激的Swi2/Snf2超家族的atp酶来完成。本文采用荧光共振能量转移（FRET）的方法研究了这种atp酶的机械化学循环，即Sulfolobus solfataricus Rad54同源物（SsoRad54cd）的催化结构域。FRET研究的结果表明，酶可以（至少）在溶液中发现两种不同的可能构象。一个开放的构象，与最近报道的晶体结构一致，在DNA结合后转化为封闭的构象。在随后的ATP结合后，FRET测量无法检测到构象的进一步变化。相反，FRET可检测的构象变化发生在ATP水解后和ADP释放之前，表明与磷酸盐释放有关的强力冲程。基于这些数据，我们将提出一种新的酶的机械化学循环模型。该方案反过来为理解Swi2/Snf2家族其他成员的功能提供了一个工作模型。
Remodelling protein nucleic acid interfaces is an important biological task, which is often carried out by nucleic acid stimulated ATPases of the Swi2/Snf2 superfamily. Here we study the mechano-chemical cycle of such an ATPase, namely the catalytic domain of the Sulfolobus solfataricus Rad54 homologue (SsoRad54cd), by means of fluorescence resonance energy transfer (FRET). The results of the FRET studies show that the enzyme can be found in (at least) two different possible conformations in solution. An open conformation, consistent with a recently reported crystal structure, is converted into a closed conformation after DNA binding. Upon subsequent binding of ATP no further change in conformation can be detected by the FRET measurements. Instead, a FRET detectable conformational change occurs after ATP hydrolysis and prior to ADP release, suggesting a powerstroke that is linked to phosphate release. Based on these data we will present a new model for the mechano-chemical cycle of this enzyme. This scheme in turn provides a working model for understanding the function of other members of the Swi2/Snf2 family.
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