Structural highlights
Publication Abstract from PubMed
We have determined the structure of Bacteroides thetaiotaomicron TetX2 at 2.8 A resolution, and shown that it is a class A flavin dependent oxidoreductase. TetX2 has broad activity against a range of tetracyclines including one of the most recent tetracyclines, tigecycline (Tygacil((R))). Comparison of TetX2 with that of the weakly homologous Pseudomonas fluorescens para-hydroxybenzoate hydroxylase (PHBH) (21% identity) shows substantial differences among residues at the substrate binding site although FAD is positioned in a similar conformation between the two enzymes and is poised to carry out catalysis.
Crystal structure of Bacteroides thetaiotaomicron TetX2: a tetracycline degrading monooxygenase at 2.8 A resolution.,Walkiewicz K, Davlieva M, Wu G, Shamoo Y Proteins. 2011 Jul;79(7):2335-40. doi: 10.1002/prot.23052. Epub 2011 May 16. PMID:21590745[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Walkiewicz K, Davlieva M, Wu G, Shamoo Y. Crystal structure of Bacteroides thetaiotaomicron TetX2: a tetracycline degrading monooxygenase at 2.8 A resolution. Proteins. 2011 Jul;79(7):2335-40. doi: 10.1002/prot.23052. Epub 2011 May 16. PMID:21590745 doi:10.1002/prot.23052