PMID:18164311
| Citation |
Li, L, Liu, X, Yang, W, Xu, F, Wang, W, Feng, L, Bartlam, M, Wang, L and Rao, Z (2008) Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase. J. Mol. Biol. 376:453-65 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1016/j.jmb.2007.11.069 |
| Keywords |
Alkane 1-Monooxygenase/analysis; Alkane 1-Monooxygenase/chemistry; Alkane 1-Monooxygenase/genetics; Alkane 1-Monooxygenase/isolation & purification; Alkane 1-Monooxygenase/metabolism; Amino Acid Sequence; Apoenzymes/chemistry; Apoenzymes/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Binding Sites; Catalysis; Crystallization; Crystallography, X-Ray; Dimerization; Escherichia coli/genetics; Flavin Mononucleotide/isolation & purification; Flavin Mononucleotide/metabolism; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Hydroxylation; Luciferases/chemistry; Luciferases/genetics; Models, Chemical; Models, Molecular; Molecular Sequence Data; Molecular Structure; Molecular Weight; Oxidation-Reduction; Point Mutation; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Sequence Homology, Amino Acid; Substrate Specificity; Water/chemistry |
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