3b9o: Difference between revisions

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[[Image:3b9o.jpg|left|200px]]
{{Seed}}
[[Image:3b9o.png|left|200px]]


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{{STRUCTURE_3b9o|  PDB=3b9o  |  SCENE=  }}  
{{STRUCTURE_3b9o|  PDB=3b9o  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_18164311}}


==About this Structure==
==About this Structure==
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Plasmid]]
[[Category: Plasmid]]
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