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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacteroides thetaiotaomicron | Q93L51 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
TetX family tetracycline inactivation enzyme | - |
Bacteroides thetaiotaomicron |
TetX2 | - |
Bacteroides thetaiotaomicron |
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 |