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A rod conformation of the Pyrococcus furiosus Rad50 coiled coil.
Proteins: Structure, Function, and Bioinformatics ( IF 2.9 ) Pub Date : 2020-09-02 , DOI: 10.1002/prot.26005
Young-Min Soh 1 , Jerome Basquin 2 , Stephan Gruber 1
Affiliation  

The Rad50‐Mre11 nuclease complex plays a vital role in DNA repair in all domains of life. It recognizes and processes DNA double‐strand breaks. Rad50 proteins fold into an extended structure with a 20 to 60 nm long coiled coil connecting a globular ABC ATPase domain with a zinc hook dimerization domain. A published structure of an archaeal Rad50 zinc hook shows coiled coils pointing away from each other. Here we present the crystal structure of an alternate conformation displaying co‐aligned coiled coils. Archaeal Rad50 may thus switch between rod‐shaped and ring‐like conformations as recently proposed for a bacterial homolog.

中文翻译:

激烈热球菌Rad50卷曲螺旋的杆构型。

Rad50-Mre11核酸酶复合物在生命的所有领域中都对DNA修复起着至关重要的作用。它识别并处理DNA双链断裂。Rad50蛋白折叠成具有20至60 nm长的卷曲螺旋的延伸结构,该螺旋卷曲将球状ABC ATPase结构域与锌钩二聚结构域相连。公开的古细菌Rad50锌钩结构显示出彼此指向相反的盘绕线圈。在这里,我们介绍了显示共排列的卷曲线圈的另一种构象的晶体结构。因此,古细菌Rad50可能会在细菌同源物的最新建议中在棒状和环状构象之间切换。
更新日期:2020-09-02
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