5ZI3
MDH3 wild type, apo-form
Summary for 5ZI3
| Entry DOI | 10.2210/pdb5zi3/pdb |
| Descriptor | Malate dehydrogenase, GLYCEROL (3 entities in total) |
| Functional Keywords | malate dehydrogenase, glyoxysome, fatty acid oxidation, mdh3, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 74940.63 |
| Authors | Moriyama, S.,Nishio, K.,Mizushima, T. (deposition date: 2018-03-14, release date: 2018-10-24, Last modification date: 2023-11-22) |
| Primary citation | Moriyama, S.,Nishio, K.,Mizushima, T. Structure of glyoxysomal malate dehydrogenase (MDH3) from Saccharomyces cerevisiae. Acta Crystallogr F Struct Biol Commun, 74:617-624, 2018 Cited by PubMed Abstract: Malate dehydrogenase (MDH), a carbohydrate and energy metabolism enzyme in eukaryotes, catalyzes the interconversion of malate to oxaloacetate (OAA) in conjunction with that of nicotinamide adenine dinucleotide (NAD) to NADH. Three isozymes of MDH have been reported in Saccharomyces cerevisiae: MDH1, MDH2 and MDH3. MDH1 is a mitochondrial enzyme and a member of the tricarboxylic acid cycle, whereas MDH2 is a cytosolic enzyme that functions in the glyoxylate cycle. MDH3 is a glyoxysomal enzyme that is involved in the reoxidation of NADH, which is produced during fatty-acid β-oxidation. The affinity of MDH3 for OAA is lower than those of MDH1 and MDH2. Here, the crystal structures of yeast apo MDH3, the MDH3-NAD complex and the MDH3-NAD-OAA ternary complex were determined. The structure of the ternary complex suggests that the active-site loop is in the open conformation, differing from the closed conformations in mitochondrial and cytosolic malate dehydrogenases. PubMed: 30279312DOI: 10.1107/S2053230X18011895 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report
