1Y7T
Crystal structure of NAD(H)-depenent malate dehydrogenase complexed with NADPH
Summary for 1Y7T
Entry DOI | 10.2210/pdb1y7t/pdb |
Related | 1BMD |
Descriptor | Malate dehydrogenase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total) |
Functional Keywords | nad-dependent-mdh-nadph complex, oxidoreductase |
Biological source | Thermus thermophilus |
Total number of polymer chains | 2 |
Total formula weight | 72912.98 |
Authors | Tomita, T.,Fushinobu, S.,Kuzuyama, T.,Nishiyama, M. (deposition date: 2004-12-10, release date: 2005-08-02, Last modification date: 2024-03-13) |
Primary citation | Tomita, T.,Fushinobu, S.,Kuzuyama, T.,Nishiyama, M. Crystal structure of NAD-dependent malate dehydrogenase complexed with NADP(H) Biochem.Biophys.Res.Commun., 334:613-618, 2005 Cited by PubMed Abstract: For better understanding of the coenzyme specificity in NAD-dependent MDH (tMDH) from Thermus flavus AT-62, we determined the crystal structures of tMDH-NADP(H) complex at maximally 1.65 A resolution. The overall structure is almost the same as that of the tMDH-NADH complex. However, NADP(H) binds to tMDH in the reverse orientation, where adenine occupies the position near the catalytic center and nicotinamide is positioned at the adenine binding site of the tMDH-NADH complex. Consistent with this, kinetic analysis of the malate-oxidizing reaction revealed that NADP(+) inhibited tMDH at high concentrations. This has provided the first evidence for the alternative binding mode of the nicotinamide coenzyme, that has pseudo-symmetry in its structure, in a single enzyme. PubMed: 16009341DOI: 10.1016/j.bbrc.2005.06.133 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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