1
Linda B. Bloom is in the Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida 32610-0245, USA
2
Myron F. Goodman is in the Department of Biological Sciences, Hedco Laboratories, University of Southern California, Los Angeles, Calfornia, 90089-1340, USA.
Correspondence should be addressed to Linda B. Bloom lbloom@ufl.edu
Crystal structures of the Escherichia coli DNA replication clamp loading complex and of a subunit of the clamp loader bound to a clamp monomer provide a physical framework in which to view ATP-dependent modulation of complex− interactions. The structural data suggest how the ring is opened and loaded onto DNA in the absence of a direct interaction between the complex and the dimer interface.
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clamp loading complex and of a subunit of the clamp loader bound to a 
clamp monomer provide a physical framework in which to view ATP-dependent modulation of 
