Structural Biochemistry and Interaction Architecture of the DNA Double-Strand Break Repair Mre11 Nuclease and Rad50-ATPase

To clarify functions of the Mre11/Rad50 (MR) complex in DNA double-strand break repair, we report Pyrococcus furiosus Mre11 crystal structures, revealing a protein phosphatase-like, dimanganese binding domain capped by a unique domain controlling active site access. These structures unify Mre11'...

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Veröffentlicht in:	Cell 2001-05, Vol.105 (4), p.473-485
Hauptverfasser:	Hopfner, Karl-Peter, Karcher, Annette, Craig, Lisa, Woo, Tammy T., Carney, James P., Tainer, John A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Archaeal Proteins - chemistry Archaeal Proteins - genetics Archaeal Proteins - metabolism ARCHITECTURE BASIC BIOLOGICAL SCIENCES Binding Sites - physiology BIOCHEMISTRY Crystallography DNA DNA - genetics DNA - metabolism DNA Repair - physiology DNA, Archaeal - genetics DNA, Archaeal - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Endodeoxyribonucleases - chemistry Endodeoxyribonucleases - genetics Endodeoxyribonucleases - metabolism Exodeoxyribonucleases - chemistry Exodeoxyribonucleases - genetics Exodeoxyribonucleases - metabolism Humans Microscopy, Electron Molecular Sequence Data Mre11 nuclease Mrell nuclease NUCLEASES Protein Structure, Tertiary Pyrococcus furiosus rad50-ATPase REPAIR
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