A polymerase I palm in adenylyl cyclase?

Peter J. Artymiuk (), Andrew R. Poirrette, David W. Rice and Peter Willett
Additional contact information
Peter J. Artymiuk: Krebs Institute, University of Sheffield
Andrew R. Poirrette: Krebs Institute, University of Sheffield
David W. Rice: Krebs Institute, University of Sheffield
Peter Willett: Krebs Institute, University of Sheffield

Nature, 1997, vol. 388, issue 6637, 33-34

Abstract: 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.

Date: 1997
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DOI: 10.1038/40310

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