4cro
From Proteopedia
PROTEIN-DNA CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURE OF A LAMBDA CRO-OPERATOR COMPLEX
Structural highlights
FunctionRCRO_LAMBD Cro represses genes normally expressed in early phage development and is necessary for the late stage of lytic growth. It does this by binding to the OL and OR operators regions normally used by the repressor protein for lysogenic maintenance. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex.,Brennan RG, Roderick SL, Takeda Y, Matthews BW Proc Natl Acad Sci U S A. 1990 Oct;87(20):8165-9. PMID:2146682[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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