1NY9

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

Summary for 1NY9

• Entry DOI: 10.2210/pdb1ny9/pdb
• Related: 1EXI 1EXJ 1JBG
• NMR Information: BMRB: 5706
• Descriptor: Transcriptional activator tipA-S (1 entity in total)
• Functional Keywords: all alpha, globin like, transcription
• Biological source: Streptomyces lividans
• Total number of polymer chains: 1
• Total formula weight: 16452.91

Authors

Kahmann, J.D.,Sass, H.J.,Allan, M.G.,Seto, H.,Thompson, C.J.,Grzesiek, S. (deposition date: 2003-02-12, release date: 2003-04-15, Last modification date: 2024-05-22)

Primary citation

Kahmann, J.D.,Sass, H.J.,Allan, M.G.,Seto, H.,Thompson, C.J.,Grzesiek, S.
Structural basis for antibiotic recognition by the TipA-class of multidrug-resistance transcriptional regulators
Embo J., 22:1824-1834, 2003

PubMed Abstract: 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.

PubMed: 12682015
DOI: 10.1093/emboj/cdg181

Experimental method

SOLUTION NMR