1PER
THE COMPLEX BETWEEN PHAGE 434 REPRESSION DNA-BINDING DOMAIN AND OPERATOR SITE OR3: STRUCTURAL DIFFERENCES BETWEEN CONSENSUS AND NON-CONSENSUS HALF-SITES
Summary for 1PER
Entry DOI | 10.2210/pdb1per/pdb |
Descriptor | DNA (5'-D(*AP*AP*GP*TP*AP*CP*AP*GP*TP*TP*TP*TP*TP*CP*TP*TP*G P*TP*AP*T)-3'), DNA (5'-D(*TP*AP*TP*AP*CP*AP*AP*GP*AP*AP*AP*AP*AP*CP*TP*GP*T P*AP*CP*T)-3'), PROTEIN (434 REPRESSOR), ... (4 entities in total) |
Functional Keywords | protein-dna complex, transcription-dna complex, transcription/dna |
Biological source | Phage 434 |
Total number of polymer chains | 4 |
Total formula weight | 27384.10 |
Authors | Rodgers, D.W.,Harrison, S.C. (deposition date: 1993-11-09, release date: 1994-01-31, Last modification date: 2024-02-14) |
Primary citation | Rodgers, D.W.,Harrison, S.C. The complex between phage 434 repressor DNA-binding domain and operator site OR3: structural differences between consensus and non-consensus half-sites. Structure, 1:227-240, 1993 Cited by PubMed Abstract: The repressor of phage 434 binds to a set of operator sites as a homodimer. Its relative affinities for these sites determine the switch from lysogenic to lytic growth. The six 434 operator sites (OR1, OR2, OR3, OL1, OL2 and OL3) have a particularly simple organization; all are 14 base pairs long, with a conserved 5'-ACAA sequence symmetrically placed at either end, and a variable central six base pairs. OR3 is unique among naturally-occurring 434 operator sites in that it contains a non-consensus base pair, G.C, at the fourth position of the otherwise invariant 5'-ACAA sequence. Comparisons among structures of the 434 repressor DNA-binding domain, R1-69, bound to various operator sites, allow us to analyze differential specificity in regulatory complexes of this kind. PubMed: 8081737DOI: 10.1016/0969-2126(93)90012-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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