3IQD
Structure of Octopine-dehydrogenase in complex with NADH and Agmatine
Summary for 3IQD
| Entry DOI | 10.2210/pdb3iqd/pdb |
| Related | 3C7A 3C7C 3C7D |
| Descriptor | Octopine dehydrogenase, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, AGMATINE (3 entities in total) |
| Functional Keywords | octopine, dehydrogenase, oxidoreductase |
| Biological source | Pecten maximus (King scallop) |
| Total number of polymer chains | 1 |
| Total formula weight | 44882.99 |
| Authors | Smits, S.H.J.,Meyer, T.,Mueller, A.,Willbold, D.,Grieshaber, M.K.,Schmitt, L. (deposition date: 2009-08-20, release date: 2010-08-25, Last modification date: 2023-11-01) |
| Primary citation | Smits, S.H.J.,Meyer, T.,Mueller, A.,van Os, N.,Stoldt, M.,Willbold, D.,Schmitt, L.,Grieshaber, M.K. Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography Plos One, 5:e12312-e12312, 2010 Cited by PubMed Abstract: Octopine dehydrogenase (OcDH) from the adductor muscle of the great scallop, Pecten maximus, catalyzes the NADH dependent, reductive condensation of L-arginine and pyruvate to octopine, NAD(+), and water during escape swimming and/or subsequent recovery. The structure of OcDH was recently solved and a reaction mechanism was proposed which implied an ordered binding of NADH, L-arginine and finally pyruvate. Here, the order of substrate binding as well as the underlying conformational changes were investigated by NMR confirming the model derived from the crystal structures. Furthermore, the crystal structure of the OcDH/NADH/agmatine complex was determined which suggests a key role of the side chain of L-arginine in protein cataylsis. Thus, the order of substrate binding to OcDH as well as the molecular signals involved in octopine formation can now be described in molecular detail. PubMed: 20808820DOI: 10.1371/journal.pone.0012312 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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