1ny9
From Proteopedia
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| Gene: | tipA (Streptomyces lividans) | ||||||
| Related: | 1EXJ, 1EXI, 1JBG
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 22:37:14 2008
