Cocrystals of the DNA-binding domain of phage 434 repressor and a synthetic phage 434 operator.
- 1 March 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (5), 1307-1311
- https://doi.org/10.1073/pnas.81.5.1307
Abstract
The amino-terminal domain of the phage 434 repressor forms cocrystals with a synthetic phage 434 operator. The cocrystals diffract to at least 4 .ANG., and X-ray crystallographic analysis of them is in progress. An analysis of the packing in the cocrystals shows that complexes consisting of dimers of amino-terminal domain bound specifically to operators are stacked end to end in long protein-DNA rods parallel to the unit cell body diagonals. The DNA in the complexes has 10.5 base pairs/turn and a rise per base of 3.26 .ANG., values consistent with B-form DNA, indicating that DNA is neither unwound nor overwound by bound repressor. The packing analysis suggests an approach that might facilitate the cocrystallization of other DNA-binding proteins with the DNA they recognize.This publication has 27 references indexed in Scilit:
- Crystallographic data for complexes of the Cro repressor with DNAJournal of Molecular Biology, 1983
- Autoregulation of the Escherichia coli crp gene: CRP is a transcriptional repressor for its own geneCell, 1983
- Proposed α-helical super-secondary structure associated with protein-DNA recognitionJournal of Molecular Biology, 1982
- Homology among DNA-binding proteins suggests use of a conserved super-secondary structureNature, 1982
- Sequence-dependent helical periodicity of DNANature, 1981
- Sequence dependence of the helical repeat of DNA in solutionNature, 1981
- Regulatory functions of the λ repressor reside in the amino-terminal domainNature, 1979
- Cooperative binding to DNA of catabolite activator protein of Escherichia coliBiochemistry, 1979
- Primary structure of the λ repressorBiochemistry, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970