1.14.13.231: tetracycline 11a-monooxygenase

This is an abbreviated version!
For detailed information about tetracycline 11a-monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.231

Reaction

RH
+
[reduced NADPH-hemoprotein reductase]
+
O2
=
ROH
+
[oxidized NADPH-hemoprotein reductase]
+
H2O

Synonyms

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

ECTree

     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
                1.14.13.231 tetracycline 11a-monooxygenase

Crystallization

Crystallization on EC 1.14.13.231 - tetracycline 11a-monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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