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1r15

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{{STRUCTURE_1r15| PDB=1r15 | SCENE= }}
{{STRUCTURE_1r15| PDB=1r15 | SCENE= }}
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'''Aplysia ADP ribosyl cyclase with bound nicotinamide and R5P'''
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===Aplysia ADP ribosyl cyclase with bound nicotinamide and R5P===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15016363 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15016363}}
==About this Structure==
==About this Structure==
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[[Category: Naadp]]
[[Category: Naadp]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:56:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:05:37 2008''

Revision as of 21:05, 27 July 2008

Image:1r15.png

Template:STRUCTURE 1r15

Aplysia ADP ribosyl cyclase with bound nicotinamide and R5P

Template:ABSTRACT PUBMED 15016363

About this Structure

1R15 is a Single protein structure of sequence from Aplysia californica. 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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