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Clamp loader ATPases and the evolution of DNA replication machinery

Brian A Kelch13*, Debora L Makino137, Mike O'Donnell6 and John Kuriyan12345

Author Affiliations

1 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA

2 Department of Chemistry, University of California, Berkeley, CA 94720, USA

3 California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA

4 Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA

5 Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA

6 Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021, USA

7 Max-Planck Institute of Biochemistry, Department of Structural Cell Biology, D-82152 Martinsried, Germany

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BMC Biology 2012, 10:34  doi:10.1186/1741-7007-10-34

Published: 20 April 2012

Additional files

Additional file 1:

The structure of the clamp loader of E. coli (known as the γ-complex) in the apo form (PDB code 1JR3).

Format: MOV Size: 7.1MB Download file

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Open Data

Additional file 2:

The structure of the budding yeast clamp loader, replication factor-C (RFC), bound to the sliding clamp, PCNA, and an ATP analog (PDB code 1SXJ).

Format: MOV Size: 10.3MB Download file

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Open Data

Additional file 3:

Movie of the T4 bacteriophage clamp loader bound to primer-template DNA, an ATP analog, and the sliding clamp during clamp closure (PDB code 3U60).

Format: MOV Size: 4.3MB Download file

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Open Data