Structural highlights
Function
[RTP_BACSU] Plays a role in DNA replication and termination (fork arrest mechanism). Two dimers of rtp bind to the two inverted repeat regions (IRI and IRII) present in the termination site. The binding of each dimer is centered on an 8 bp direct repeat.
Publication Abstract from PubMed
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.
Structure of the RTP-DNA complex and the mechanism of polar replication fork arrest.,Wilce JA, Vivian JP, Hastings AF, Otting G, Folmer RH, Duggin IG, Wake RG, Wilce MC Nat Struct Biol. 2001 Mar;8(3):206-10. PMID:11224562[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wilce JA, Vivian JP, Hastings AF, Otting G, Folmer RH, Duggin IG, Wake RG, Wilce MC. Structure of the RTP-DNA complex and the mechanism of polar replication fork arrest. Nat Struct Biol. 2001 Mar;8(3):206-10. PMID:11224562 doi:10.1038/84934
