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Article
Nature 290, 744-749 (30 April 1981) | doi:10.1038/290744a0; Received 3 November 1980; Accepted 24 February 1981
Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA
David B. McKay & Thomas A. Steitz
- Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
Abstract
The 2.9 Å resolution crystal structure of Escherichia coli catabolite gene activator protein (CAP) completed with cyclic AMP reveals two distinct structural domains separated by a cleft. The smaller carboxy-terminal domain is presumed to bind DNA while the amino-terminal domain is seen to bind cyclic AMP. Model building studies suggest that CAP binds to left-handed B-type DNA, contacting its major groove via two a-helices. It is possible that the CAP conversion of right- to left-handed DNA in a closed supercoil, is what activates transcription by RNA polymerase.
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