1bm9
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(New page: 200px<br /><applet load="1bm9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bm9, resolution 2.00Å" /> '''REPLICATION TERMINAT...)
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Revision as of 09:38, 20 November 2007
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REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS
Overview
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.
About this Structure
1BM9 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
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
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