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Journal Article

A rod conformation of the Pyrococcus furiosus Rad50 coiled coil

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Basquin,  Jerome
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Soh, Y.-M., Basquin, J., & Gruber, S. (2020). A rod conformation of the Pyrococcus furiosus Rad50 coiled coil. Proteins, 89, 1-5. doi:10.1002/prot.26005.


Cite as: https://hdl.handle.net/21.11116/0000-0007-828C-8
Abstract
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 60nm 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. © 2020 Wiley Periodicals LLC.