6N2N
Crystal structure of 2-oxoglutarate:ferredoxin oxidoreductase from Magnetococcus marinus
6N2N の概要
エントリーDOI | 10.2210/pdb6n2n/pdb |
関連するPDBエントリー | 6N2O |
分子名称 | Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein, Pyruvate ferredoxin/flavodoxin oxidoreductase, beta subunit, SULFATE ION, ... (7 entities in total) |
機能のキーワード | thiamine pyrophosphate, [4fe-4s] cluster, carbon fixation, reductive tricarboxylic acid cycle, rtca, 2-oxoglutarate:ferredoxin oxidoreductase, electron transfer, oxidoreductase |
由来する生物種 | Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1) 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 189718.70 |
構造登録者 | |
主引用文献 | Chen, P.Y.,Li, B.,Drennan, C.L.,Elliott, S.J. A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes C-C bonds from CO2. Joule, 3:595-611, 2019 Cited by PubMed Abstract: 2-oxoglutarate:ferredoxin oxidoreductase (OGOR) is a thiamine pyrophosphate (TPP) and [4Fe-4S] cluster-dependent enzyme from the reductive tricarboxylic acid (rTCA) cycle that fixes CO to succinyl-CoA, forming 2-oxoglutarate and CoA. Here we report an OGOR from the rTCA cycle of MC-1, along with all three potential ferredoxin (Fd) redox partners. We demonstrate OGOR operates bidirectionally (both CO-fixing and 2-oxoglutarate oxidizing), and that only one Fd (Fd1) supports efficient catalysis. Our 1.94-Å and 2.80-Å resolution crystal structures of native and substrate-bound forms of OGOR reveal the determinants of substrate specificity and CoA-binding in an OGOR, and illuminate the [4Fe-4S] cluster environment, portraying the electronic conduit allowing Fd1 to be wired to the bound-TPP. Structural and biochemical data further identify Glu45α as a mobile residue that impacts catalytic bias toward CO-fixation although it makes no direct contact with TPP-bound intermediates, indicating that reaction directionality can be tuned by second layer interactions. (149 of 150 words limit). PubMed: 31080943DOI: 10.1016/j.joule.2018.12.006 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.937 Å) |
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