Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks
Article Abstract:
The crystal structure of RecBCD bound to a DNA substrate is presented. The DNA duplex is split across the RecC subunit to create a fork with the separated strands each heading towards different helicase motor subunits. The strands pass along tunnels within the complex, both emerging adjacent to the nuclease domain of RecB.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover
Article Abstract:
The crystal structures of the catalytic domain of Escherichia coli RNase E are reported as trapped allosteric intermediates with RNA substrates. The subdomain encompassing the active site is structurally congruent to a deoxyribonuclease that makes an unexpected link in the evolutionary history of RNA and DNA nucleases.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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RecBCD enzyme is a bipolar DNA helicase
Article Abstract:
Experiments are performed to find the relation between the RecBCD enzyme and DNA helicases. The reasons why RecB and RecD are both active in intact RecBCD are mentioned.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2003
User Contributions:
Comment about this article or add new information about this topic:
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