2EFW

Crystal structure of the RTP:nRB complex from Bacillus subtilis

Summary for 2EFW

• Entry DOI: 10.2210/pdb2efw/pdb
• Related: 1F4K 1J0R 1bm9
• Descriptor: DNA (5'-D(*DCP*DT*DAP*DTP*DGP*DTP*DAP*DCP*DCP*DAP*DAP*DAP*DTP*DGP*DTP*DTP*DCP*DAP*DGP*DTP*DC)-3'), DNA (5'-D(*DGP*DAP*DCP*DTP*DGP*DAP*DAP*DCP*DAP*DTP*DTP*DTP*DGP*DGP*DTP*DAP*DCP*DAP*DTP*DAP*DG)-3'), Replication termination protein, ... (4 entities in total)
• Functional Keywords: protein-dna complex, 'winged'-helix protein, dna replication termination, replication fork arrest, replication-dna complex, replication/dna
• Biological source: Bacillus subtilis
• Total number of polymer chains: 8
• Total formula weight: 83891.16

Authors

Vivian, J.P.,Porter, C.J.,Wilce, J.A.,Wilce, M.C.J. (deposition date: 2007-02-26, release date: 2008-02-26, Last modification date: 2023-10-25)

Primary citation

Vivian, J.P.,Porter, C.J.,Wilce, J.A.,Wilce, M.C.J.
An asymmetric structure of the Bacillus subtilis replication terminator protein in complex with DNA
J.Mol.Biol., 370:481-491, 2007

PubMed Abstract: In Bacillus subtilis, the termination of DNA replication via polar fork arrest is effected by a specific protein:DNA complex formed between the replication terminator protein (RTP) and DNA terminator sites. We report the crystal structure of a replication terminator protein homologue (RTP.C110S) of B. subtilis in complex with the high affinity component of one of its cognate DNA termination sites, known as the TerI B-site, refined at 2.5 A resolution. The 21 bp RTP:DNA complex displays marked structural asymmetry in both the homodimeric protein and the DNA. This is in contrast to the previously reported complex formed with a symmetrical TerI B-site homologue. The induced asymmetry is consistent with the complex's solution properties as determined using NMR spectroscopy. Concomitant with this asymmetry is variation in the protein:DNA binding pattern for each of the subunits of the RTP homodimer. It is proposed that the asymmetric "wing" positions, as well as other asymmetrical features of the RTP:DNA complex, are critical for the cooperative binding that underlies the mechanism of polar fork arrest at the complete terminator site.

PubMed: 17521668
DOI: 10.1016/j.jmb.2007.02.067

Experimental method

X-RAY DIFFRACTION (2.5 Å)