1r0s: Difference between revisions
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==Crystal structure of ADP-ribosyl cyclase Glu179Ala mutant== | ==Crystal structure of ADP-ribosyl cyclase Glu179Ala mutant== | ||
<StructureSection load='1r0s' size='340' side='right' caption='[[1r0s]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1r0s' size='340' side='right'caption='[[1r0s]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1r0s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aplca Aplca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R0S FirstGlance]. <br> | <table><tr><td colspan='2'>[[1r0s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aplca Aplca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R0S FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Aplca]] | [[Category: Aplca]] | ||
[[Category: Large Structures]] | |||
[[Category: Graeff, R]] | [[Category: Graeff, R]] | ||
[[Category: Hao, Q]] | [[Category: Hao, Q]] | ||
Revision as of 14:36, 4 December 2019
Crystal structure of ADP-ribosyl cyclase Glu179Ala mutantCrystal structure of ADP-ribosyl cyclase Glu179Ala mutant
Structural highlights
Function[NADA_APLCA] Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for calcium mobilization from endoplasmic reticulum. Also has cADPr hydrolase activity.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedADP-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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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