1bm9

REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILISREPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS

Structural highlights 1bm9 is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 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. Crystal structure of the replication terminator protein from B. subtilis at 2.6 A.,Bussiere DE, Bastia D, White SW Cell. 1995 Feb 24;80(4):651-60. PMID:7867072 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Replication Termination Protein

spinqualitylabelsall models 1bm9, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image