Abstract
The crystal structure of the replication terminator protein (RTP) of B. subtilis has been determined at 2.6 Å resolution. As previously suggested by both biochemical and biophysical studies, the molecule exists as a symmetric dimer and is in the α+β protein-folding class. The protein has several uncommon features, including an antiparallel coiled-coil, which serves as the dimerization domain, and both an α-helix and a β-ribbon suitably positioned to interact with the major and minor grooves of B-DNA. A site has been identified on the surface of RTP that is biochemically and positionally suitable for interaction with the replication-specific helicase. Other features of the structure are consistent with the polar contrahelicase mechanism of the protein. A model of the interaction between RTP and its cognate DNA is presented.
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