5ULV の概要
| エントリーDOI | 10.2210/pdb5ulv/pdb |
| 分子名称 | Malate dehydrogenase, CALCIUM ION (3 entities in total) |
| 機能のキーワード | malate, dehydrogenase, nad, oxidoreductase |
| 由来する生物種 | Methylobacterium extorquens |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 33761.80 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.66 Å) |
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