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Article: The homo-dimeric form of ADP-ribosyl cyclase in solution

TitleThe homo-dimeric form of ADP-ribosyl cyclase in solution
Authors
Issue Date1998
Citation
Biochimica Et Biophysica Acta - Protein Structure And Molecular Enzymology, 1998, v. 1388 n. 2, p. 428-436 How to Cite?
AbstractADP-ribosyl cyclase is a multi-functional enzyme that catalyzes the formation of two Ca2+ signaling molecules, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP). X-ray crystallography of three different crystal forms shows that it is a non-covalent dimer. Chemical cross-linking and dynamic light scattering were used in this study to determine if the cyclase is also a non-covalent dimer in solution. Treatment of the cyclase in dilute solution (0.05 mg/ml) with dimethylsuberimidate resulted in complete conversion to a species with molecular weight about twice that of the monomeric cyclase. Prolonged cross-linking of the cyclase at four times higher concentration produced also only the covalently linked dimers and no multimer formation was observed. The cross-linked dimer retained full enzymatic activity and readily catalyzed the formation of cADPR from NAD, NAADP from NADP, cyclic ADP-ribose phosphate from NADP, and cyclic GDP-ribose from nicotinamide guanine dinucleotide. Analysis of the autocorrelation functions obtained from dynamic light scattering measurements indicated the cyclase solution (2 mg/ml) was composed of a single molecular species and its diffusion coefficient was measured to be 7.4x10-7 cm2/s. Computer modeling using the crystallographic dimensions of the non-covalent cyclase dimer, a donut shaped molecule with a central cavity and overall dimensions of 7x6x3 nm, gave a value for the diffusion coefficient essentially the same as that measured. These results indicate the cyclase is a non-covalent dimer in solution. Copyright (C) 1998 Elsevier Science B.V.
Persistent Identifierhttp://hdl.handle.net/10722/171655
ISSN
2004 Impact Factor: 3.079
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMunshi, Cen_US
dc.contributor.authorBaumann, Cen_US
dc.contributor.authorLevitt, Den_US
dc.contributor.authorBloomfield, VAen_US
dc.contributor.authorLee, HCen_US
dc.date.accessioned2012-10-30T06:16:11Z-
dc.date.available2012-10-30T06:16:11Z-
dc.date.issued1998en_US
dc.identifier.citationBiochimica Et Biophysica Acta - Protein Structure And Molecular Enzymology, 1998, v. 1388 n. 2, p. 428-436en_US
dc.identifier.issn0167-4838en_US
dc.identifier.urihttp://hdl.handle.net/10722/171655-
dc.description.abstractADP-ribosyl cyclase is a multi-functional enzyme that catalyzes the formation of two Ca2+ signaling molecules, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP). X-ray crystallography of three different crystal forms shows that it is a non-covalent dimer. Chemical cross-linking and dynamic light scattering were used in this study to determine if the cyclase is also a non-covalent dimer in solution. Treatment of the cyclase in dilute solution (0.05 mg/ml) with dimethylsuberimidate resulted in complete conversion to a species with molecular weight about twice that of the monomeric cyclase. Prolonged cross-linking of the cyclase at four times higher concentration produced also only the covalently linked dimers and no multimer formation was observed. The cross-linked dimer retained full enzymatic activity and readily catalyzed the formation of cADPR from NAD, NAADP from NADP, cyclic ADP-ribose phosphate from NADP, and cyclic GDP-ribose from nicotinamide guanine dinucleotide. Analysis of the autocorrelation functions obtained from dynamic light scattering measurements indicated the cyclase solution (2 mg/ml) was composed of a single molecular species and its diffusion coefficient was measured to be 7.4x10-7 cm2/s. Computer modeling using the crystallographic dimensions of the non-covalent cyclase dimer, a donut shaped molecule with a central cavity and overall dimensions of 7x6x3 nm, gave a value for the diffusion coefficient essentially the same as that measured. These results indicate the cyclase is a non-covalent dimer in solution. Copyright (C) 1998 Elsevier Science B.V.en_US
dc.languageengen_US
dc.relation.ispartofBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymologyen_US
dc.subject.meshAdp-Ribosyl Cyclaseen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntigens, Cden_US
dc.subject.meshAntigens, Cd38en_US
dc.subject.meshAntigens, Differentiation - Chemistryen_US
dc.subject.meshAplysia - Enzymologyen_US
dc.subject.meshCross-Linking Reagents - Metabolismen_US
dc.subject.meshDimerizationen_US
dc.subject.meshDimethyl Suberimidate - Metabolismen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshGuanine Nucleotides - Metabolismen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshKineticsen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshNad - Analogs & Derivatives - Metabolismen_US
dc.subject.meshNad+ Nucleosidase - Chemistryen_US
dc.subject.meshNadp - Metabolismen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshScattering, Radiationen_US
dc.titleThe homo-dimeric form of ADP-ribosyl cyclase in solutionen_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0167-4838(98)00204-0en_US
dc.identifier.pmid9858777-
dc.identifier.scopuseid_2-s2.0-0032506274en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032506274&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume1388en_US
dc.identifier.issue2en_US
dc.identifier.spage428en_US
dc.identifier.epage436en_US
dc.identifier.isiWOS:000077105900014-
dc.identifier.scopusauthoridMunshi, C=7003972383en_US
dc.identifier.scopusauthoridBaumann, C=7101777922en_US
dc.identifier.scopusauthoridLevitt, D=7102923276en_US
dc.identifier.scopusauthoridBloomfield, VA=7005771347en_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US

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