1BM9

REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS

Summary for 1BM9

• Entry DOI: 10.2210/pdb1bm9/pdb
• Descriptor: REPLICATION TERMINATOR PROTEIN (2 entities in total)
• Functional Keywords: dna-binding protein, contrahelicase, dna binding protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 29094.33

Authors

Bussiere, D.E.,Bastia, D.,White, S. (deposition date: 1998-07-29, release date: 1999-01-06, Last modification date: 2024-02-07)

Primary citation

Bussiere, D.E.,Bastia, D.,White, S.W.
Crystal structure of the replication terminator protein from B. subtilis at 2.6 A.
Cell(Cambridge,Mass.), 80:651-660, 1995

PubMed Abstract: The crystal structure of the replication terminator protein (RTP) of B. subtilis has been determined at 2.6 A resolution. As previously suggested by both biochemical and biophysical studies, the molecule exists as a symmetric dimer and is in the alpha + beta protein-folding class. The protein has several uncommon features, including an antiparallel coiled-coil, which serves as the dimerization domain, and both an alpha-helix and a beta-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.

PubMed: 7867072
DOI: 10.1016/0092-8674(95)90519-7

Experimental method

X-RAY DIFFRACTION (2 Å)