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

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...

Full description

Saved in:
Bibliographic Details
Published inNature structural biology Vol. 3; no. 11; p. 957
Main Authors Prasad, G S, McRee, D E, Stura, E A, Levitt, D G, Lee, H C, Stout, C D
Format Journal Article
LanguageEnglish
Published United States 01.11.1996
Subjects
Adenosine Diphosphate Ribose - metabolism
ADP-ribosyl Cyclase
ADP-ribosyl Cyclase 1
Amino Acid Sequence
Animals
Antigens, CD
Antigens, Differentiation - chemistry
Aplysia - enzymology
Conserved Sequence
Crystallography, X-Ray
Dimerization
GPI-Linked Proteins
Membrane Glycoproteins - chemistry
Models, Molecular
Molecular Sequence Data
N-Glycosyl Hydrolases - chemistry
Protein Conformation
Sequence Homology, Amino Acid
Online AccessGet more information

Cover

More Information
Summary: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.
ISSN:1072-8368
DOI:10.1038/nsb1196-957