| Literature DB >> 11224562 |
J A Wilce1, J P Vivian, A F Hastings, G Otting, R H Folmer, I G Duggin, R G Wake, M C Wilce.
Abstract
The coordinated termination of DNA replication is an important step in the life cycle of bacteria with circular chromosomes, but has only been defined at a molecular level in two systems to date. Here we report the structure of an engineered replication terminator protein (RTP) of Bacillus subtilis in complex with a 21 base pair DNA by X-ray crystallography at 2.5 A resolution. We also use NMR spectroscopic titration techniques. This work reveals a novel DNA interaction involving a dimeric 'winged helix' domain protein that differs from predictions. While the two recognition helices of RTP are in close contact with the B-form DNA major grooves, the 'wings' and N-termini of RTP do not form intimate contacts with the DNA. This structure provides insight into the molecular basis of polar replication fork arrest based on a model of cooperative binding and differential binding affinities of RTP to the two adjacent binding sites in the complete terminator.Entities:
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Year: 2001 PMID： 11224562 DOI： 10.1038/84934
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368