1F4K

CRYSTAL STRUCTURE OF THE REPLICATION TERMINATOR PROTEIN/B-SITE DNA COMPLEX

Summary for 1F4K

• Entry DOI: 10.2210/pdb1f4k/pdb
• Related: 1BM9
• Descriptor: 5'-D(*CP*TP*AP*TP*GP*AP*AP*CP*AP*TP*AP*AP*TP*GP*TP*TP*CP*AP*TP*AP*G)-3', 5'-D(*CP*TP*AP*TP*GP*AP*AP*CP*AP*TP*TP*AP*TP*GP*TP*TP*CP*AP*TP*AP*G)-3', REPLICATION TERMINATION PROTEIN, ... (4 entities in total)
• Functional Keywords: winged-helix protein-dna complex, replication and termination, fork arrest mechanism, replication-dna complex, replication/dna
• Biological source: Bacillus subtilis
• Total number of polymer chains: 4
• Total formula weight: 41943.60

Authors

Wilce, J.A.,Vivian, J.P.,Hastings, A.F.,Otting, G.,Folmer, R.H.A.,Duggin, I.G.,Wake, R.G.,Wilce, M.C.J. (deposition date: 2000-06-08, release date: 2001-06-08, Last modification date: 2024-02-07)

Primary citation

Wilce, J.A.,Vivian, J.P.,Hastings, A.F.,Otting, G.,Folmer, R.H.,Duggin, I.G.,Wake, R.G.,Wilce, M.C.
Structure of the RTP-DNA complex and the mechanism of polar replication fork arrest
Nat.Struct.Biol., 8:206-210, 2001

PubMed 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.

PubMed: 11224562
DOI: 10.1038/84934

Experimental method

X-RAY DIFFRACTION (2.5 Å)