1lbe: Difference between revisions

Revision as of 12:13, 2 July 2008

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File:1lbe.png

Template:STRUCTURE 1lbe

APLYSIA ADP RIBOSYL CYCLASEAPLYSIA ADP RIBOSYL CYCLASE

Template:ABSTRACT PUBMED 8901875

About this StructureAbout this Structure

1LBE is a Single protein structure of sequence from Aplysia californica. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38., Prasad GS, McRee DE, Stura EA, Levitt DG, Lee HC, Stout CD, Nat Struct Biol. 1996 Nov;3(11):957-64. PMID:8901875

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OCA

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-'''APLYSIA ADP RIBOSYL CYCLASE'''
+===APLYSIA ADP RIBOSYL CYCLASE===
-==Overview==
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-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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 [[Category: Hydrolase]]
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