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

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: 8107872
DOI: 10.1038/367754a0

Experimental method

X-RAY DIFFRACTION (2.6 Å)