Abstract
Zhang et al.1 recently reported the long-awaited structure determination of one of the catalytic core domains of eukaryotic adenylyl cyclase, which promises a greater understanding of the regulatory mechanisms associated with the use of cyclic AMP as a second messenger. We have searched the Brookhaven Protein Data Bank2 using the program PROTEP3 and found that, far from having a completely novel fold, the fold of the domain bears an extraordinary resemblance to the ‘palm’ domains of the polymerase I family of prokaryotic DNA polymerases, including Escherichia coli DNA polymerase I4,5 and Thermus aquaticus ( Taq) polymerase6,7. The similarity has important implications for the function and evolution of eukaryotic adenylyl cyclases and related proteins.
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Artymiuk, P., Poirrette, A., Rice, D. et al. A polymerase I palm in adenylyl cyclase?. Nature 388, 33–34 (1997). https://doi.org/10.1038/40310
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DOI: https://doi.org/10.1038/40310
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