1lbe

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(New page: 200px<br /><applet load="1lbe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lbe, resolution 2.4&Aring;" /> '''APLYSIA ADP RIBOSYL C...)
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Revision as of 18:19, 20 November 2007

Image:1lbe.gif

1lbe, resolution 2.4Å

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APLYSIA ADP RIBOSYL CYCLASE

Overview

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.

About this Structure

1LBE is a Single protein structure of sequence from Aplysia californica. Active as NAD(+) nucleosidase, with EC number 3.2.2.5 Full crystallographic information is available from OCA.

Reference

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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