1r16
From Proteopedia
(New page: 200px<br /><applet load="1r16" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r16, resolution 2.0Å" /> '''Aplysia ADP ribosyl c...) |
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| - | [[Image:1r16.jpg|left|200px]]<br /><applet load="1r16" size=" | + | [[Image:1r16.jpg|left|200px]]<br /><applet load="1r16" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r16, resolution 2.0Å" /> | caption="1r16, resolution 2.0Å" /> | ||
'''Aplysia ADP ribosyl cyclase with bound pyridylcarbinol and R5P'''<br /> | '''Aplysia ADP ribosyl cyclase with bound pyridylcarbinol and R5P'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ADP-ribosyl cyclase catalyzes the elimination of nicotinamide from NAD and | + | ADP-ribosyl cyclase catalyzes the elimination of nicotinamide from NAD and cyclization to cADPR, a known second messenger in cellular calcium signaling pathways. We have determined to 2.0 A resolution the structure of Aplysia cyclase with ribose-5-phosphate bound covalently at C3' and with the base exchange substrate (BES), pyridylcarbinol, bound to the active site. In addition, further refinement at 2.4 A resolution of the structure of nicotinamide-bound cyclase, which was previously reported, reveals that ribose-5-phosphate is also covalently bound in this structure, and a second nicotinamide site was identified. The structures of native and mutant Glu179Ala cyclase were also solved to 1.7 and 2.0 A respectively. It is proposed that the second nicotinamide site serves to promote cyclization by clearing the active site of the nicotinamide byproduct. Moreover, a ribosylation mechanism can be proposed in which the cyclization reaction proceeds through a covalently bound intermediate. |
==About this Structure== | ==About this Structure== | ||
| - | 1R16 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica] with ROB and PYF as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1R16 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica] with <scene name='pdbligand=ROB:'>ROB</scene> and <scene name='pdbligand=PYF:'>PYF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1R16 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Graeff, R.]] | [[Category: Graeff, R.]] | ||
[[Category: Hao, Q.]] | [[Category: Hao, Q.]] | ||
| - | [[Category: Kriksunov, I | + | [[Category: Kriksunov, I A.]] |
| - | [[Category: Lee, H | + | [[Category: Lee, H C.]] |
| - | [[Category: Love, M | + | [[Category: Love, M L.]] |
[[Category: Munshi, C.]] | [[Category: Munshi, C.]] | ||
| - | [[Category: Szebenyi, D | + | [[Category: Szebenyi, D M.E.]] |
| - | [[Category: Thiel, D | + | [[Category: Thiel, D J.]] |
[[Category: PYF]] | [[Category: PYF]] | ||
[[Category: ROB]] | [[Category: ROB]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:54 2008'' |
Revision as of 12:45, 21 February 2008
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Aplysia ADP ribosyl cyclase with bound pyridylcarbinol and R5P
Overview
ADP-ribosyl cyclase catalyzes the elimination of nicotinamide from NAD and cyclization to cADPR, a known second messenger in cellular calcium signaling pathways. We have determined to 2.0 A resolution the structure of Aplysia cyclase with ribose-5-phosphate bound covalently at C3' and with the base exchange substrate (BES), pyridylcarbinol, bound to the active site. In addition, further refinement at 2.4 A resolution of the structure of nicotinamide-bound cyclase, which was previously reported, reveals that ribose-5-phosphate is also covalently bound in this structure, and a second nicotinamide site was identified. The structures of native and mutant Glu179Ala cyclase were also solved to 1.7 and 2.0 A respectively. It is proposed that the second nicotinamide site serves to promote cyclization by clearing the active site of the nicotinamide byproduct. Moreover, a ribosylation mechanism can be proposed in which the cyclization reaction proceeds through a covalently bound intermediate.
About this Structure
1R16 is a Single protein structure of sequence from Aplysia californica with and as ligands. Active as NAD(+) nucleosidase, with EC number 3.2.2.5 Full crystallographic information is available from OCA.
Reference
ADP-ribosyl cyclase; crystal structures reveal a covalent intermediate., Love ML, Szebenyi DM, Kriksunov IA, Thiel DJ, Munshi C, Graeff R, Lee HC, Hao Q, Structure. 2004 Mar;12(3):477-86. PMID:15016363
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