1LBE

APLYSIA ADP RIBOSYL CYCLASE

Summary for 1LBE

• Entry DOI: 10.2210/pdb1lbe/pdb
• Descriptor: ADP RIBOSYL CYCLASE (2 entities in total)
• Functional Keywords: hydrolase, nad(+) nucleosidase, nadase
• Biological source: Aplysia californica (California sea hare)
• Cellular location: Cytoplasmic vesicle: P29241
• Total number of polymer chains: 2
• Total formula weight: 59159.89

Authors

Prasad, G.S.,Mcree, D.E.,Stura, E.A.,Levitt, D.G.,Lee, H.C.,Stout, C.D. (deposition date: 1996-09-18, release date: 1997-09-17, Last modification date: 2011-07-13)

Primary citation

Prasad, G.S.,McRee, D.E.,Stura, E.A.,Levitt, D.G.,Lee, H.C.,Stout, C.D.
Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38.
Nat.Struct.Biol., 3:957-964, 1996

PubMed 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.

PubMed: 8901875
DOI: 10.1038/nsb1196-957

Experimental method

X-RAY DIFFRACTION (2.4 Å)