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3B9O

long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN

3B9O の概要
エントリーDOI10.2210/pdb3b9o/pdb
関連するPDBエントリー3B9N
分子名称Alkane monooxygenase, FLAVIN MONONUCLEOTIDE (3 entities in total)
機能のキーワードgeobacillus thermodenitrificans, lada, alkane hydroxylase, monooxygenase, plasmid, oxidoreductase
由来する生物種Geobacillus thermodenitrificans
タンパク質・核酸の鎖数2
化学式量合計101992.93
構造登録者
Li, L.,Yang, W.,Xu, F.,Bartlam, M.,Rao, Z. (登録日: 2007-11-06, 公開日: 2008-01-15, 最終更新日: 2023-11-01)
主引用文献Li, L.,Liu, X.,Yang, W.,Xu, F.,Wang, W.,Feng, L.,Bartlam, M.,Wang, L.,Rao, Z.
Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase
J.Mol.Biol., 376:453-465, 2008
Cited by
PubMed Abstract: LadA, a long-chain alkane monooxygenase, utilizes a terminal oxidation pathway for the conversion of long-chain alkanes (up to at least C(36)) to corresponding primary alcohols in thermophilic bacillus Geobacillus thermodenitrificans NG80-2. Here, we report the first structure of the long-chain alkane hydroxylase, LadA, and its complex with the flavin mononucleotide (FMN) coenzyme. LadA is characterized as a new member of the SsuD subfamily of the bacterial luciferase family via a surprising structural relationship. The LadA:FMN binary complex structure and a LadA:FMN:alkane model reveal a hydrophobic cavity that has dual roles: to provide a hydrogen-bond donor (His138) for catalysis and to create a solvent-free environment in which to stabilize the C4a-hydroperoxyflavin intermediate. Consequently, LadA should catalyze the conversion of long-chain alkanes via the acknowledged flavoprotein monooxygenase mechanism. This finding suggests that the ability of LadA to catalyze the degradation of long-chain alkanes is determined by the binding mode of the long-chain alkane substrates. The LadA structure opens a rational perspective to explore and alter the substrate binding site of LadA, with potential biotechnological applications in areas such as petroleum exploration and treatment of environmental oil pollution.
PubMed: 18164311
DOI: 10.1016/j.jmb.2007.11.069
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 3b9o
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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