1r0s: Difference between revisions
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'''Crystal structure of ADP-ribosyl cyclase Glu179Ala mutant''' | {{Structure | ||
|PDB= 1r0s |SIZE=350|CAPTION= <scene name='initialview01'>1r0s</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of ADP-ribosyl cyclase Glu179Ala mutant''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1R0S is a [ | 1R0S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0S OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15016363 15016363] | ||
[[Category: Aplysia californica]] | [[Category: Aplysia californica]] | ||
[[Category: NAD(+) nucleosidase]] | [[Category: NAD(+) nucleosidase]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:45:18 2008'' | ||
Revision as of 14:45, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Activity: | NAD(+) nucleosidase, with EC number 3.2.2.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of ADP-ribosyl cyclase Glu179Ala mutant
OverviewOverview
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 StructureAbout this Structure
1R0S is a Single protein structure of sequence from Aplysia californica. Full crystallographic information is available from OCA.
ReferenceReference
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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