1PAR
DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL STRUCTURE
Summary for 1PAR
Entry DOI | 10.2210/pdb1par/pdb |
Descriptor | DNA (5'-D(*TP*AP*TP*AP*GP*TP*AP*GP*AP*GP*TP*GP*CP*TP*TP*CP*T P*AP*TP*CP*AP*T)- 3'), DNA (5'-D(*AP*AP*TP*GP*AP*TP*AP*GP*AP*AP*GP*CP*AP*CP*TP*CP*T P*AP*CP*TP*AP*T)- 3'), PROTEIN (ARC REPRESSOR), ... (4 entities in total) |
Functional Keywords | protein-dna complex, double helix, transcription-dna complex, transcription/dna |
Biological source | Enterobacteria phage P22 |
Total number of polymer chains | 6 |
Total formula weight | 38452.88 |
Authors | Raumann, B.E.,Rould, M.A.,Pabo, C.O.,Sauer, R.T. (deposition date: 1994-03-22, release date: 1994-07-31, Last modification date: 2024-02-14) |
Primary citation | Raumann, B.E.,Rould, M.A.,Pabo, C.O.,Sauer, R.T. DNA recognition by beta-sheets in the Arc repressor-operator crystal structure. Nature, 367:754-757, 1994 Cited by PubMed Abstract: 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. PubMed: 8107872DOI: 10.1038/367754a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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