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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA.

The 2.9 A resolution crystal structure of Escherichia coli catabolite gene activator protein (CAP) complexed 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, contracting its major groove via two alpha-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.[1]

References

  1. Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA. McKay, D.B., Steitz, T.A. Nature (1981) [Pubmed]
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