A rod conformation of the Pyrococcus furiosus Rad50 coiled coil.

Details

Serval ID
serval:BIB_E5C92095B881
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
A rod conformation of the Pyrococcus furiosus Rad50 coiled coil.
Journal
Proteins
Author(s)
Soh Y.M., Basquin J., Gruber S.
ISSN
1097-0134 (Electronic)
ISSN-L
0887-3585
Publication state
Published
Issued date
02/09/2020
Peer-reviewed
Oui
Language
english
Notes
Publication types: Journal Article
Publication Status: aheadofprint
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 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.
Keywords
DNA repair, Mre11, Rad50, SMC, SMC-like, coiled coil, rod, zinc hook
Pubmed
Web of science
Create date
15/09/2020 9:55
Last modification date
27/10/2020 6:26
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