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

Nat Struct Biol. 1996 Nov;3(11):957-64. doi: 10.1038/nsb1196-957.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • ADP-ribosyl Cyclase
  • ADP-ribosyl Cyclase 1
  • Adenosine Diphosphate Ribose / metabolism
  • 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

Substances

  • Antigens, CD
  • Antigens, Differentiation
  • GPI-Linked Proteins
  • Membrane Glycoproteins
  • Adenosine Diphosphate Ribose
  • N-Glycosyl Hydrolases
  • ADP-ribosyl Cyclase
  • ADP-ribosyl cyclase 2
  • ADP-ribosyl Cyclase 1