1ny9

Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulatorAntibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator

Structural highlights 1ny9 is a 1 chain structure with sequence from Streptomyces lividans. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TIPA_STRLI Transcriptional activator. Is activated when bound to the antibiotic thiostrepton. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcriptional activator 3D structures

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