1ny9: Difference between revisions
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'''Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator'''<br /> | '''Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator'''<br /> | ||
==Overview== | ==Overview== | ||
The TipAL protein, a bacterial transcriptional regulator of the MerR | 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== | ==About this Structure== | ||
1NY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http:// | 1NY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NY9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces lividans]] | [[Category: Streptomyces lividans]] | ||
[[Category: Allan, M | [[Category: Allan, M G.]] | ||
[[Category: Grzesiek, S.]] | [[Category: Grzesiek, S.]] | ||
[[Category: Kahmann, J | [[Category: Kahmann, J D.]] | ||
[[Category: Sass, H | [[Category: Sass, H J.]] | ||
[[Category: Seto, H.]] | [[Category: Seto, H.]] | ||
[[Category: Thompson, C | [[Category: Thompson, C J.]] | ||
[[Category: all alpha]] | [[Category: all alpha]] | ||
[[Category: globin like]] | [[Category: globin like]] | ||
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Revision as of 12:11, 21 February 2008
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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
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