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  A rod conformation of the Pyrococcus furiosus Rad50 coiled coil

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

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Genre: Journal Article

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 Creators:
Soh, Young-Min1, Author
Basquin, Jerome2, Author              
Gruber, Stephan1, Author
Affiliations:
1external, ou_persistent22              
2Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: DNA repair; Mre11; Rad50; SMC; SMC-like; coiled coil; rod; zinc hook
 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.

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Language(s): eng - English
 Dates: 2020-09
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: ACKNOWLEDGEMENTS
We are grateful to the Crystallization Facility at the Max Planck Institute of Biochemistry.
 Rev. Type: -
 Identifiers: ISI: 32875643
DOI: 10.1002/prot.26005
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Project name : -
Grant ID : 724482
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)

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Title: Proteins
Source Genre: Journal
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Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 1 - 5 Identifier: ISSN: 1097-0134