tetracycline 11a-monooxygenase

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Word Map on EC


[reduced NADPH-hemoprotein reductase]
[oxidized NADPH-hemoprotein reductase]


BN1088_100004, tetracycline resistance protein from transposon Tn4351/Tn4400, tetracylcine resistance protein TetX, TetX, TetX family tetracycline inactivation enzyme, TetX2


     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
       tetracycline 11a-monooxygenase


Crystallization on EC - tetracycline 11a-monooxygenase

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in complex with tetracyclines minocycline and tigecycline at 2.18 and 2.30 A resolution, respectively. Both tetracyclines bind in a large tunnel-shaped active site in close contact to the cofactor FAD, preoriented for regioselective hydroxylation to 11alpha-hydroxytetracyclines. The bulky 9-tert-butylglycylamido substituent of tigecycline is solvent-exposed and does not interfere with TetX binding. In the TetX-minocycline complex a second binding site for a minocycline dimer is observed close to the active-site entrance. The putative dioxygen-binding cavities are located in the substrate-binding domain next to the active site
structure at 2.8 A resolution and comparison with that of the weakly homologous Pseudomonas fluorescens parahydroxybenzoate hydroxylase
structure determinations at 2.1 A resolution of native TetX and its complexes with tetracyclines. Domain 1 exhibits the Rossmann fold responsible for binding of the coenzyme FAD through its adenosine monophosphate component, which is linked to the flavin mononucleotide containing the catalytically active isoalloxazine moiety. The second domain with an extended 7-stranded beta-sheet is positioned like a shield on top of the flavin-binding domain covered by five alpha-helices and is responsible for substrate recognition. A long C-terminal alpha-helix stabilizes the association of the two domains