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Nature Structural Biology  10, 496 - 498 (2003)
doi:10.1038/nsb0703-496

Remodeling of replication initiator proteins

Katrina T Forest & Marcin S Filutowicz

The authors are in the Department of Bacteriology, University of Wisconsin-Madison, 420 Henry Mall, Madison, Wisconsin 53706, USA. forest@bact.wisc.edu

The structure of the dimeric replication initiator of pPS10 reveals that secondary structure remodeling of chameleon sequences defines the monomer-dimer oligomerization state of the protein. Together with an unanticipated dimerization interface, this result will steer thinking in the field and influence strategies to control spread of virulence and antibiotic resistance genes that are often plasmid-encoded.

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RESEARCH
A conformational switch between transcriptional repression and replication initiation in the RepA dimerization domain
Nature Structural Biology Article (01 Jul 2003)
Crystal structure of a prokaryotic replication initiator protein bound to DNA at 2.6 Å resolution
The EMBO Journal Article (01 Sep 1999)

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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