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'''DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL STRUCTURE''' | '''DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL STRUCTURE''' | ||
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[[Category: Rould, M A.]] | [[Category: Rould, M A.]] | ||
[[Category: Sauer, R T.]] | [[Category: Sauer, R T.]] | ||
[[Category: | [[Category: Double helix]] | ||
[[Category: | [[Category: Protein-dna complex]] | ||
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Revision as of 04:53, 3 May 2008
DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL STRUCTURE
OverviewOverview
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 StructureAbout this Structure
1PAR is a Single protein structure of sequence from Enterobacteria phage p22. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 04:53:24 2008