The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch.

The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch.
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DOI:
10.1074/jbc.c900018200
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发表时间:
2009-04-17
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
Schüler H
Schüler H
中科院分区:
其他
文献类型:
--
作者:
Collins R;Karlberg T;Lehtiö L;Schütz P;van den Berg S;Dahlgren LG;Hammarström M;Weigelt J;Schüler H

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DEXD/H-box RNA解旋酶通过未知机制将ATP水解与RNA重塑偶联。我们使用X射线晶体学和生化分析的人DEXD/H-box蛋白DDX 19,以研究其调节机制。DDX 19在其RNA结合的预水解和游离的水解后状态下的晶体结构显示,在游离蛋白的保守结构域之间插入α-螺旋,以负调节ATP酶活性。这一发现得到了生化数据的证实,证实了蛋白质的N-末端区域的自动调节功能。这是第一个描述DEXD/H-box蛋白在其开放和闭合裂缝构象中的晶体结构的研究。
DEXD/H-box RNA helicases couple ATP hydrolysis to RNA remodeling by an unknown mechanism. We used x-ray crystallography and biochemical analysis of the human DEXD/H-box protein DDX19 to investigate its regulatory mechanism. The crystal structures of DDX19, in its RNA-bound prehydrolysis and free posthydrolysis state, reveal an α-helix that inserts between the conserved domains of the free protein to negatively regulate ATPase activity. This finding was corroborated by biochemical data that confirm an autoregulatory function of the N-terminal region of the protein. This is the first study describing crystal structures of a DEXD/H-box protein in its open and closed cleft conformations.