1lbe
From Proteopedia
(New page: 200px<br /><applet load="1lbe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lbe, resolution 2.4Å" /> '''APLYSIA ADP RIBOSYL C...) |
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| - | [[Image:1lbe.gif|left|200px]]<br /><applet load="1lbe" size=" | + | [[Image:1lbe.gif|left|200px]]<br /><applet load="1lbe" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lbe, resolution 2.4Å" /> | caption="1lbe, resolution 2.4Å" /> | ||
'''APLYSIA ADP RIBOSYL CYCLASE'''<br /> | '''APLYSIA ADP RIBOSYL CYCLASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ADP ribosyl cyclase synthesizes the novel secondary messenger cyclic ADP | + | 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== | ==About this Structure== | ||
| - | 1LBE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Active as [http://en.wikipedia.org/wiki/NAD(+)_nucleosidase NAD(+) nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.5 3.2.2.5] Full crystallographic information is available from [http:// | + | 1LBE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Active as [http://en.wikipedia.org/wiki/NAD(+)_nucleosidase NAD(+) nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.5 3.2.2.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: NAD(+) nucleosidase]] | [[Category: NAD(+) nucleosidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lee, H | + | [[Category: Lee, H C.]] |
| - | [[Category: Levitt, D | + | [[Category: Levitt, D G.]] |
| - | [[Category: Mcree, D | + | [[Category: Mcree, D E.]] |
| - | [[Category: Prasad, G | + | [[Category: Prasad, G S.]] |
| - | [[Category: Stout, C | + | [[Category: Stout, C D.]] |
| - | [[Category: Stura, E | + | [[Category: Stura, E A.]] |
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: nad(+) nucleosidase]] | [[Category: nad(+) nucleosidase]] | ||
[[Category: nadase]] | [[Category: nadase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:22 2008'' |
Revision as of 11:43, 21 February 2008
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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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