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New page: left|200px<br /><applet load="1f4k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f4k, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1f4k.gif|left|200px]]<br /><applet load="1f4k" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1f4k.gif|left|200px]]<br /><applet load="1f4k" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1f4k, resolution 2.5&Aring;" />
caption="1f4k, resolution 2.5&Aring;" />
'''CRYSTAL STRUCTURE OF THE REPLICATION TERMINATOR PROTEIN/B-SITE DNA COMPLEX'''<br />
'''CRYSTAL STRUCTURE OF THE REPLICATION TERMINATOR PROTEIN/B-SITE DNA COMPLEX'''<br />


==Overview==
==Overview==
The coordinated termination of DNA replication is an important step in the, life cycle of bacteria with circular chromosomes, but has only been, defined at a molecular level in two systems to date. Here we report the, structure of an engineered replication terminator protein (RTP) of, Bacillus subtilis in complex with a 21 base pair DNA by X-ray, crystallography at 2.5 A resolution. We also use NMR spectroscopic, titration techniques. This work reveals a novel DNA interaction involving, a dimeric 'winged helix' domain protein that differs from predictions., While the two recognition helices of RTP are in close contact with the, B-form DNA major grooves, the 'wings' and N-termini of RTP do not form, intimate contacts with the DNA. This structure provides insight into the, molecular basis of polar replication fork arrest based on a model of, cooperative binding and differential binding affinities of RTP to the two, adjacent binding sites in the complete terminator.
The coordinated termination of DNA replication is an important step in the life cycle of bacteria with circular chromosomes, but has only been defined at a molecular level in two systems to date. Here we report the structure of an engineered replication terminator protein (RTP) of Bacillus subtilis in complex with a 21 base pair DNA by X-ray crystallography at 2.5 A resolution. We also use NMR spectroscopic titration techniques. This work reveals a novel DNA interaction involving a dimeric 'winged helix' domain protein that differs from predictions. While the two recognition helices of RTP are in close contact with the B-form DNA major grooves, the 'wings' and N-termini of RTP do not form intimate contacts with the DNA. This structure provides insight into the molecular basis of polar replication fork arrest based on a model of cooperative binding and differential binding affinities of RTP to the two adjacent binding sites in the complete terminator.


==About this Structure==
==About this Structure==
1F4K 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=1F4K OCA].  
1F4K 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=1F4K OCA].  


==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Duggin, I.G.]]
[[Category: Duggin, I G.]]
[[Category: Folmer, R.H.A.]]
[[Category: Folmer, R H.A.]]
[[Category: Hastings, A.F.]]
[[Category: Hastings, A F.]]
[[Category: Otting, G.]]
[[Category: Otting, G.]]
[[Category: Vivian, J.P.]]
[[Category: Vivian, J P.]]
[[Category: Wake, R.G.]]
[[Category: Wake, R G.]]
[[Category: Wilce, J.A.]]
[[Category: Wilce, J A.]]
[[Category: Wilce, M.C.J.]]
[[Category: Wilce, M C.J.]]
[[Category: fork arrest mechanism]]
[[Category: fork arrest mechanism]]
[[Category: replication and termination]]
[[Category: replication and termination]]
[[Category: winged-helix protein-dna complex]]
[[Category: winged-helix protein-dna complex]]


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