4CRO

PROTEIN-DNA CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURE OF A LAMBDA CRO-OPERATOR COMPLEX

Summary for 4CRO

• Entry DOI: 10.2210/pdb4cro/pdb
• Descriptor: DNA (5'-D(*TP*AP*TP*CP*AP*CP*CP*GP*CP*GP*GP*GP*TP*GP*AP*TP*A)-3'), PROTEIN (LAMBDA CRO) (2 entities in total)
• Functional Keywords: protein-dna complex, double helix, transcription-dna complex, transcription/dna
• Biological source: Enterobacteria phage lambda
• Total number of polymer chains: 12
• Total formula weight: 75617.29

Authors

Brennan, R.G.,Roderick, S.L.,Takeda, Y.,Matthews, B.W. (deposition date: 1992-01-15, release date: 1992-01-15, Last modification date: 2022-11-23)

Primary citation

Brennan, R.G.,Roderick, S.L.,Takeda, Y.,Matthews, B.W.
Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex.
Proc.Natl.Acad.Sci.USA, 87:8165-8169, 1990

PubMed Abstract: The structure of a complex of bacteriophage lambda Cro protein with a 17-base-pair operator has been determined at 3.9-A resolution. Isomorphous derivatives obtained by the synthesis of site-specific iodinated DNA oligomers were of critical importance in solving the structure. The crystal structure contains three independent Cro-operator complexes that have very similar, although not necessarily identical, conformations. In the complex, the protein dimer undergoes a large conformational change relative to the crystal structure of the free protein. One monomer rotates by about 40 degrees relative to the other, this being accomplished primarily by a twisting of the two beta-sheet strands that connect one monomer with the other. In the complex, the DNA is bent by about 40 degrees into the shape of a boomerang but maintains essentially Watson-Crick B-form. In contrast to other known protein-DNA complexes, the DNA is not stacked end-to-end. The structure confirms the general features of the model previously proposed for the interaction of Cro with DNA.

PubMed: 2146682
DOI: 10.1073/pnas.87.20.8165

Experimental method

X-RAY DIFFRACTION (3.9 Å)