Summary for 5ULV
| Entry DOI | 10.2210/pdb5ulv/pdb |
| Descriptor | Malate dehydrogenase, CALCIUM ION (3 entities in total) |
| Functional Keywords | malate, dehydrogenase, nad, oxidoreductase |
| Biological source | Methylobacterium extorquens |
| Total number of polymer chains | 1 |
| Total formula weight | 33761.80 |
| Authors | Gonzalez, J.M. (deposition date: 2017-01-25, release date: 2017-02-08, Last modification date: 2023-10-04) |
| Primary citation | Gonzalez, J.M.,Marti-Arbona, R.,Chen, J.C.H.,Broom-Peltz, B.,Unkefer, C.J. Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase. Acta Crystallogr F Struct Biol Commun, 74:610-616, 2018 Cited by PubMed Abstract: Three high-resolution X-ray crystal structures of malate dehydrogenase (MDH; EC 1.1.1.37) from the methylotroph Methylobacterium extorquens AM1 are presented. By comparing the structures of apo MDH, a binary complex of MDH and NAD, and a ternary complex of MDH and oxaloacetate with ADP-ribose occupying the pyridine nucleotide-binding site, conformational changes associated with the formation of the catalytic complex were characterized. While the substrate-binding site is accessible in the enzyme resting state or NAD-bound forms, the substrate-bound form exhibits a closed conformation. This conformational change involves the transition of an α-helix to a 3-helix, which causes the adjacent loop to close the active site following coenzyme and substrate binding. In the ternary complex, His284 forms a hydrogen bond to the C2 carbonyl of oxaloacetate, placing it in a position to donate a proton in the formation of (2S)-malate. PubMed: 30279311DOI: 10.1107/S2053230X18011809 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.66 Å) |
Structure validation
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