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

G. Sridhar Prasad, Duncan E. McRee, Enrico A. Stura, David G Levitt, Hon Cheung Lee, C. David Stout

Research output: Contribution to journalArticle

137 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)957-964
Number of pages8
JournalNature Structural Biology
Volume3
Issue number11
DOIs
StatePublished - Nov 1 1996

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    Prasad, G. S., McRee, D. E., Stura, E. A., Levitt, D. G., Lee, H. C., & Stout, C. D. (1996). Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38. Nature Structural Biology, 3(11), 957-964. https://doi.org/10.1038/nsb1196-957