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Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38

Nature Structural Biology volume 3, pages 957–964 (1996)Cite this article

Abstract

ADP ribosyl cyclase synthesizes the novel secondary messenger cyclic ADP ribose (cADPR) utilizing NAD as a substrate. The enzyme shares extensive sequence similarity with two lymphocyte antigens, CD38 and BST-1, which hydrolyse as well as synthesize cADPR. The crystal structure provides a model for these cell surface enzymes. Cyclase contains two spatially separated pockets composed of sequence conserved residues, suggesting that the cyclization reaction may entail use of distinct sites. The enzyme dimer encloses a cavity which may entrap the intermediate, ADP ribose.

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Authors and Affiliations

  1. Department of Molecular Biology, The Scripps Research Institute, La Jolla, California, 92037, USA

    G. Sridhar Prasad, Duncan E. McRee, Enrico A. Stura & C. David Stout

  2. Department of Physiology, University of Minnesota, Minneapolis, Minnesota, 55455, USA

    David G. Levitt & Hon Cheung Lee

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Prasad, G., McRee, D., Stura, E. et al. Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38. Nat Struct Mol Biol 3, 957–964 (1996). https://doi.org/10.1038/nsb1196-957

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