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.
© 2020 Wiley Periodicals LLC.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Archaeal Proteins / chemistry*
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Archaeal Proteins / genetics
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Archaeal Proteins / metabolism
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Binding Sites
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Cations, Divalent
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Cloning, Molecular
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Crystallography, X-Ray
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DNA Repair*
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DNA, Archaeal / chemistry*
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DNA, Archaeal / genetics
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DNA, Archaeal / metabolism
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Endodeoxyribonucleases / chemistry*
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Endodeoxyribonucleases / genetics
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Endodeoxyribonucleases / metabolism
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Exodeoxyribonucleases / chemistry*
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Exodeoxyribonucleases / genetics
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Exodeoxyribonucleases / metabolism
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Gene Expression
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Genetic Vectors / chemistry
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Genetic Vectors / metabolism
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Humans
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Models, Molecular
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Protein Binding
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Protein Conformation, alpha-Helical
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Protein Interaction Domains and Motifs
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Protein Multimerization
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Pyrococcus furiosus / genetics*
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Pyrococcus furiosus / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Structural Homology, Protein
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Zinc / chemistry*
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Zinc / metabolism
Substances
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Archaeal Proteins
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Cations, Divalent
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DNA, Archaeal
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Recombinant Proteins
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Endodeoxyribonucleases
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Exodeoxyribonucleases
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Mre11 protein, archaeal
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Rad50 protein, archaeal
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Zinc