+検索条件
-Structure paper
タイトル | Structural basis for enzymatic terminal C-H bond functionalization of alkanes. |
---|---|
ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 30, Issue 4, Page 521-526, Year 2023 |
掲載日 | 2023年3月30日 |
著者 | Jin Chai / Gongrui Guo / Sean M McSweeney / John Shanklin / Qun Liu / |
PubMed 要旨 | Alkane monooxygenase (AlkB) is a widely occurring integral membrane metalloenzyme that catalyzes the initial step in the functionalization of recalcitrant alkanes with high terminal selectivity. AlkB ...Alkane monooxygenase (AlkB) is a widely occurring integral membrane metalloenzyme that catalyzes the initial step in the functionalization of recalcitrant alkanes with high terminal selectivity. AlkB enables diverse microorganisms to use alkanes as their sole carbon and energy source. Here we present the 48.6-kDa cryo-electron microscopy structure of a natural fusion from Fontimonas thermophila between AlkB and its electron donor AlkG at 2.76 Å resolution. The AlkB portion contains six transmembrane helices with an alkane entry tunnel within its transmembrane domain. A dodecane substrate is oriented by hydrophobic tunnel-lining residues to present a terminal C-H bond toward a diiron active site. AlkG, an [Fe-4S] rubredoxin, docks via electrostatic interactions and sequentially transfers electrons to the diiron center. The archetypal structural complex presented reveals the basis for terminal C-H selectivity and functionalization within this broadly distributed evolutionary class of enzymes. |
リンク | Nat Struct Mol Biol / PubMed:36997762 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.76 Å |
構造データ | EMDB-28890, PDB-8f6t: |
化合物 | ChemComp-FE: ChemComp-D12: |
由来 |
|
キーワード | OXIDOREDUCTASE / Electron transfer complex / iron-sulfur cluster / histidine-diiron center / hydrophobic alkane binding pocket |