1R15
Aplysia ADP ribosyl cyclase with bound nicotinamide and R5P
Summary for 1R15
| Entry DOI | 10.2210/pdb1r15/pdb |
| Related | 1ISG 1ISH 1ISI 1ISJ 1ISM 1LBE 1R0S 1R12 1R16 |
| Descriptor | ADP-ribosyl cyclase, ANY 5'-MONOPHOSPHATE NUCLEOTIDE, NICOTINAMIDE (3 entities in total) |
| Functional Keywords | adp-ribosyl cyclase, cyclic adp-ribose, naadp, ca2+ signalling, hydrolase |
| Biological source | Aplysia californica (California sea hare) |
| Cellular location | Cytoplasmic vesicle: P29241 |
| Total number of polymer chains | 8 |
| Total formula weight | 240306.44 |
| Authors | Love, M.L.,Szebenyi, D.M.E.,Kriksunov, I.A.,Thiel, D.J.,Munshi, C.,Graeff, R.,Lee, H.C.,Hao, Q. (deposition date: 2003-09-23, release date: 2004-03-09, Last modification date: 2024-10-16) |
| Primary citation | Love, M.L.,Szebenyi, D.M.,Kriksunov, I.A.,Thiel, D.J.,Munshi, C.,Graeff, R.,Lee, H.C.,Hao, Q. ADP-ribosyl cyclase; crystal structures reveal a covalent intermediate. Structure, 12:477-486, 2004 Cited by PubMed Abstract: 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. PubMed: 15016363DOI: 10.1016/j.str.2004.02.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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