1par
From Proteopedia
(New page: 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=" | + | [[Image:1par.gif|left|200px]]<br /><applet load="1par" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1par, resolution 2.600Å" /> | caption="1par, resolution 2.600Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Pabo, C O.]] |
| - | [[Category: Raumann, B | + | [[Category: Raumann, B E.]] |
| - | [[Category: Rould, M | + | [[Category: Rould, M A.]] |
| - | [[Category: Sauer, R | + | [[Category: Sauer, R T.]] |
[[Category: double helix]] | [[Category: double helix]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:54 2008'' |
Revision as of 12:26, 21 February 2008
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DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL STRUCTURE
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.
About this Structure
1PAR is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.
Reference
DNA recognition by beta-sheets in the Arc repressor-operator crystal structure., Raumann BE, Rould MA, Pabo CO, Sauer RT, Nature. 1994 Feb 24;367(6465):754-7. PMID:8107872
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