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1lbe

From Proteopedia

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[[Image:1lbe.gif|left|200px]]
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{{STRUCTURE_1lbe| PDB=1lbe | SCENE= }}
{{STRUCTURE_1lbe| PDB=1lbe | SCENE= }}
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'''APLYSIA ADP RIBOSYL CYCLASE'''
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===APLYSIA ADP RIBOSYL CYCLASE===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 8901875 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8901875}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Nadase]]
[[Category: Nadase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:45:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:13:49 2008''

Revision as of 09:13, 2 July 2008

Image:1lbe.png

Template:STRUCTURE 1lbe

APLYSIA ADP RIBOSYL CYCLASE

Template:ABSTRACT PUBMED 8901875

About this Structure

1LBE is a Single protein structure of sequence from Aplysia californica. 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

Page seeded by OCA on Wed Jul 2 12:13:49 2008

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