1ny9

Publication Abstract from PubMed

The TipAL protein, a bacterial transcriptional regulator of the MerR family, is activated by numerous cyclic thiopeptide antibiotics. Its C-terminal drug-binding domain, TipAS, defines a subfamily of broadly distributed bacterial proteins including Mta, a central regulator of multidrug resistance in Bacillus subtilis. The structure of apo TipAS, solved by solution NMR [Brookhaven Protein Data Bank entry 1NY9], is composed of a globin-like alpha-helical fold with a deep surface cleft and an unfolded N-terminal region. Antibiotics bind within the cleft at a position that is close to the corresponding heme pocket in myo- and hemoglobin, and induce folding of the N-terminus. Thus the classical globin fold is well adapted not only for accommodating its canonical cofactors, heme and other tetrapyrroles, but also for the recognition of a variety of antibiotics where ligand binding leads to transcriptional activation and drug resistance.

Structural basis for antibiotic recognition by the TipA class of multidrug-resistance transcriptional regulators.,Kahmann JD, Sass HJ, Allan MG, Seto H, Thompson CJ, Grzesiek S EMBO J. 2003 Apr 15;22(8):1824-34. PMID:12682015^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.