1ny9
From Proteopedia
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Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator
Overview
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.
About this Structure
1NY9 is a Single protein structure of sequence from Streptomyces lividans. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 22:39:18 2007
