1bm9: Difference between revisions

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New page: left|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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[[Image:1bm9.jpg|left|200px]]<br /><applet load="1bm9" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1bm9.jpg|left|200px]]<br /><applet load="1bm9" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1bm9, resolution 2.00&Aring;" />
caption="1bm9, resolution 2.00&Aring;" />
'''REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS'''<br />
'''REPLICATION TERMINATOR PROTEIN FROM BACILLUS SUBTILIS'''<br />


==Overview==
==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.
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==
==About this Structure==
1BM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BM9 OCA].  
1BM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM9 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bastia, D.]]
[[Category: Bastia, D.]]
[[Category: Bussiere, D.E.]]
[[Category: Bussiere, D E.]]
[[Category: White, S.]]
[[Category: White, S.]]
[[Category: contrahelicase]]
[[Category: contrahelicase]]
[[Category: dna-binding protein]]
[[Category: dna-binding protein]]


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