8SBB

Cryo-EM structure of FtAlkB

8SBB の概要

• エントリーDOI: 10.2210/pdb8sbb/pdb
• EMDBエントリー: 40303
• 分子名称: Alkane 1-monooxygenase, Nanobody, FE (III) ION, ... (4 entities in total)
• 機能のキーワード: enzyme, membrane protein
• 由来する生物種: Fontimonas thermophila; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60353.54

構造登録者

Zhang, J.,Feng, L. (登録日: 2023-04-03, 公開日: 2023-04-26, 最終更新日: 2025-05-28)

主引用文献

Guo, X.,Zhang, J.,Han, L.,Lee, J.,Williams, S.C.,Forsberg, A.,Xu, Y.,Austin, R.N.,Feng, L.
Structure and mechanism of the alkane-oxidizing enzyme AlkB.
Nat Commun, 14:2180-2180, 2023

PubMed Abstract: Alkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle. Alkane monooxygenase (AlkB), a membrane-spanning metalloenzyme, converts straight chain alkanes to alcohols in the first step of the microbially-mediated degradation of alkanes, thereby playing a critical role in the global cycling of carbon and the bioremediation of oil. AlkB biodiversity is attributed to its ability to oxidize alkanes of various chain lengths, while individual AlkBs target a relatively narrow range. Mechanisms of substrate selectivity and catalytic activity remain elusive. Here we report the cryo-EM structure of AlkB, which provides a distinct architecture for membrane enzymes. Our structure and functional studies reveal an unexpected diiron center configuration and identify molecular determinants for substrate selectivity. These findings provide insight into the catalytic mechanism of AlkB and shed light on its function in alkane-degrading microorganisms.

PubMed: 37069165
DOI: 10.1038/s41467-023-37869-z

実験手法

ELECTRON MICROSCOPY (3.59 Å)