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The CTPase activity of ParB determines the size and dynamics of prokaryotic DNA partition complexes
Affiliation:1. Department of Biology, University of Marburg, 35043 Marburg, Germany;2. Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany;3. Department of Chemistry, University of Marburg, 35043 Marburg, Germany;4. Center for Synthetic Microbiology, 35043 Marburg, Germany;5. Theoretical Chemistry, Ruhr University Bochum, 44801 Bochum, Germany;6. Department of Microbiology and Molecular Medicine, University of Geneva, 1211 Geneva, Switzerland;7. Department of Systems & Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany;8. Institute for General Microbiology, Christian Albrechts University, 24118 Kiel, Germany
Abstract:
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  • Keywords:ParA  nucleotide-binding protein  ParB/sulfiredoxin domain  ParB/Srx domain  ParB-like nuclease domain  NTPase  nucleotide hydrolysis  nucleotide-binding site  water wire
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