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

doi:10.1038/nsb1196-957

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

Integrative Biology and Physiology

Research output: Contribution to journal › Article › peer-review

140 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 language	English (US)
Pages (from-to)	957-964
Number of pages	8
Journal	Nature Structural Biology
Volume	3
Issue number	11
DOIs	https://doi.org/10.1038/nsb1196-957
State	Published - Nov 1996

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

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.",

author = "Prasad, {G. Sridhar} and McRee, {Duncan E.} and Stura, {Enrico A.} and Levitt, {David G} and Lee, {Hon Cheung} and Stout, {C. David}",

year = "1996",

month = nov,

doi = "10.1038/nsb1196-957",

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AU - Prasad, G. Sridhar

AU - McRee, Duncan E.

AU - Stura, Enrico A.

AU - Levitt, David G

AU - Lee, Hon Cheung

AU - Stout, C. David

PY - 1996/11

Y1 - 1996/11

N2 - 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.

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

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