Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.13.231 extracted from

  • Volkers, G.; Palm, G.J.; Weiss, M.S.; Wright, G.D.; Hinrichs, W.
    Structural basis for a new tetracycline resistance mechanism relying on the TetX monooxygenase (2011), FEBS Lett., 585, 1061-1066.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Bacteroides thetaiotaomicron

Organism

Organism UniProt Comment Textmining
Bacteroides thetaiotaomicron Q93L51
-
-

Synonyms

Synonyms Comment Organism
TetX family tetracycline inactivation enzyme
-
Bacteroides thetaiotaomicron
TetX2
-
Bacteroides thetaiotaomicron

Cofactor

Cofactor Comment Organism Structure
FAD FAD is bound non-covalently in an elongated, so-called IN conformation with the adenine and isoalloxazine moieties distal to each other Bacteroides thetaiotaomicron