1par: Difference between revisions

New page: left|200px<br /><applet load="1par" size="450" color="white" frame="true" align="right" spinBox="true" caption="1par, resolution 2.600Å" /> '''DNA RECOGNITION BY ...
 
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[[Image:1par.gif|left|200px]]<br /><applet load="1par" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1par.gif|left|200px]]<br /><applet load="1par" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1par, resolution 2.600&Aring;" />
caption="1par, resolution 2.600&Aring;" />
'''DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL STRUCTURE'''<br />
'''DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL STRUCTURE'''<br />


==Overview==
==Overview==
Transcription of the ant gene during lytic growth of bacteriophage P22, (ref. 1) is regulated by the cooperative binding of two Arc repressor, dimers to a 21-base-pair operator site. Here we report the co-crystal, structure of this Arc tetramer-operator complex at 2.6 A resolution. As, expected from genetic and structural studies and from the co-crystal, structure of the homologous Escherichia coli MetJ repressor, each Arc, dimer uses an antiparallel beta-sheet to recognize bases in the major, groove. However, the Arc and MetJ complexes differ in several important, ways: the beta-sheet-DNA interactions of Arc are far less symmetrical; DNA, binding by Arc is accompanied by important conformational changes in the, beta-sheet; and Arc uses a different part of its protein surface for, dimer-dimer interactions.
Transcription of the ant gene during lytic growth of bacteriophage P22 (ref. 1) is regulated by the cooperative binding of two Arc repressor dimers to a 21-base-pair operator site. Here we report the co-crystal structure of this Arc tetramer-operator complex at 2.6 A resolution. As expected from genetic and structural studies and from the co-crystal structure of the homologous Escherichia coli MetJ repressor, each Arc dimer uses an antiparallel beta-sheet to recognize bases in the major groove. However, the Arc and MetJ complexes differ in several important ways: the beta-sheet-DNA interactions of Arc are far less symmetrical; DNA binding by Arc is accompanied by important conformational changes in the beta-sheet; and Arc uses a different part of its protein surface for dimer-dimer interactions.


==About this Structure==
==About this Structure==
1PAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PAR OCA].  
1PAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PAR OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Yersinia phage py54]]
[[Category: Yersinia phage py54]]
[[Category: Pabo, C.O.]]
[[Category: Pabo, C O.]]
[[Category: Raumann, B.E.]]
[[Category: Raumann, B E.]]
[[Category: Rould, M.A.]]
[[Category: Rould, M A.]]
[[Category: Sauer, R.T.]]
[[Category: Sauer, R T.]]
[[Category: double helix]]
[[Category: double helix]]
[[Category: protein-dna complex]]
[[Category: protein-dna complex]]


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