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Article: ADP-ribosyl cyclase: Crystal structures reveal a covalent intermediate

TitleADP-ribosyl cyclase: Crystal structures reveal a covalent intermediate
Authors
Issue Date2004
PublisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/str
Citation
Structure, 2004, v. 12 n. 3, p. 477-486 How to Cite?
AbstractADP-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 Å 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 Å 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 Å 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.
Persistent Identifierhttp://hdl.handle.net/10722/91911
ISSN
2015 Impact Factor: 5.237
2015 SCImago Journal Rankings: 4.770
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLove, MLen_HK
dc.contributor.authorSzebenyi, DMEen_HK
dc.contributor.authorKriksunov, IAen_HK
dc.contributor.authorThiel, DJen_HK
dc.contributor.authorMunshi, Cen_HK
dc.contributor.authorGraeff, Ren_HK
dc.contributor.authorLee, HCen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:30:18Z-
dc.date.available2010-09-17T10:30:18Z-
dc.date.issued2004en_HK
dc.identifier.citationStructure, 2004, v. 12 n. 3, p. 477-486en_HK
dc.identifier.issn0969-2126en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91911-
dc.description.abstractADP-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 Å 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 Å 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 Å 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.en_HK
dc.languageengen_HK
dc.publisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/stren_HK
dc.relation.ispartofStructureen_HK
dc.titleADP-ribosyl cyclase: Crystal structures reveal a covalent intermediateen_HK
dc.typeArticleen_HK
dc.identifier.emailGraeff, R: graeffr@hku.hken_HK
dc.identifier.emailLee, HC: leehc@hku.hken_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityGraeff, R=rp01464en_HK
dc.identifier.authorityLee, HC=rp00545en_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.str.2004.02.006en_HK
dc.identifier.pmid15016363-
dc.identifier.scopuseid_2-s2.0-1542581553en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-1542581553&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume12en_HK
dc.identifier.issue3en_HK
dc.identifier.spage477en_HK
dc.identifier.epage486en_HK
dc.identifier.isiWOS:000221430300015-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLove, ML=7004467130en_HK
dc.identifier.scopusauthoridSzebenyi, DME=6603230617en_HK
dc.identifier.scopusauthoridKriksunov, IA=6507909504en_HK
dc.identifier.scopusauthoridThiel, DJ=7005794841en_HK
dc.identifier.scopusauthoridMunshi, C=7003972383en_HK
dc.identifier.scopusauthoridGraeff, R=7003614053en_HK
dc.identifier.scopusauthoridLee, HC=26642959100en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK

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