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A polymerase I palm in adenylyl cyclase?

Author

Listed:
  • 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)

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.

Suggested Citation

  • Peter J. Artymiuk & Andrew R. Poirrette & David W. Rice & Peter Willett, 1997. "A polymerase I palm in adenylyl cyclase?," Nature, Nature, vol. 388(6637), pages 33-34, July.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6637:d:10.1038_40310
    DOI: 10.1038/40310
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