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- Publisher Website: 10.1016/S0167-4838(98)00204-0
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- PMID: 9858777
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Article: The homo-dimeric form of ADP-ribosyl cyclase in solution
Title | The homo-dimeric form of ADP-ribosyl cyclase in solution |
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Authors | |
Keywords | ADP-ribosyl cyclase CD38 Crystallographic structure Cyclic ADP-ribose Dynamic laser-light scattering |
Issue Date | 1998 |
Citation | Biochimica Et Biophysica Acta - Protein Structure And Molecular Enzymology, 1998, v. 1388 n. 2, p. 428-436 How to Cite? |
Abstract | ADP-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 Identifier | http://hdl.handle.net/10722/171655 |
ISSN | |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Munshi, C | en_US |
dc.contributor.author | Baumann, C | en_US |
dc.contributor.author | Levitt, D | en_US |
dc.contributor.author | Bloomfield, VA | en_US |
dc.contributor.author | Lee, HC | en_US |
dc.date.accessioned | 2012-10-30T06:16:11Z | - |
dc.date.available | 2012-10-30T06:16:11Z | - |
dc.date.issued | 1998 | en_US |
dc.identifier.citation | Biochimica Et Biophysica Acta - Protein Structure And Molecular Enzymology, 1998, v. 1388 n. 2, p. 428-436 | en_US |
dc.identifier.issn | 0167-4838 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171655 | - |
dc.description.abstract | ADP-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.language | eng | en_US |
dc.relation.ispartof | Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology | en_US |
dc.subject | ADP-ribosyl cyclase | - |
dc.subject | CD38 | - |
dc.subject | Crystallographic structure | - |
dc.subject | Cyclic ADP-ribose | - |
dc.subject | Dynamic laser-light scattering | - |
dc.subject.mesh | Adp-Ribosyl Cyclase | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Antigens, Cd | en_US |
dc.subject.mesh | Antigens, Cd38 | en_US |
dc.subject.mesh | Antigens, Differentiation - Chemistry | en_US |
dc.subject.mesh | Aplysia - Enzymology | en_US |
dc.subject.mesh | Cross-Linking Reagents - Metabolism | en_US |
dc.subject.mesh | Dimerization | en_US |
dc.subject.mesh | Dimethyl Suberimidate - Metabolism | en_US |
dc.subject.mesh | Electrophoresis, Polyacrylamide Gel | en_US |
dc.subject.mesh | Guanine Nucleotides - Metabolism | en_US |
dc.subject.mesh | Hydrogen-Ion Concentration | en_US |
dc.subject.mesh | Kinetics | en_US |
dc.subject.mesh | Models, Molecular | en_US |
dc.subject.mesh | Nad - Analogs & Derivatives - Metabolism | en_US |
dc.subject.mesh | Nad+ Nucleosidase - Chemistry | en_US |
dc.subject.mesh | Nadp - Metabolism | en_US |
dc.subject.mesh | Protein Conformation | en_US |
dc.subject.mesh | Scattering, Radiation | en_US |
dc.title | The homo-dimeric form of ADP-ribosyl cyclase in solution | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lee, HC:leehc@hku.hk | en_US |
dc.identifier.authority | Lee, HC=rp00545 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1016/S0167-4838(98)00204-0 | en_US |
dc.identifier.pmid | 9858777 | - |
dc.identifier.scopus | eid_2-s2.0-0032506274 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0032506274&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 1388 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.spage | 428 | en_US |
dc.identifier.epage | 436 | en_US |
dc.identifier.isi | WOS:000077105900014 | - |
dc.identifier.scopusauthorid | Munshi, C=7003972383 | en_US |
dc.identifier.scopusauthorid | Baumann, C=7101777922 | en_US |
dc.identifier.scopusauthorid | Levitt, D=7102923276 | en_US |
dc.identifier.scopusauthorid | Bloomfield, VA=7005771347 | en_US |
dc.identifier.scopusauthorid | Lee, HC=26642959100 | en_US |
dc.identifier.issnl | 0167-4838 | - |