1ny9: Difference between revisions
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[[Image:1ny9.jpg|left|200px]] | [[Image:1ny9.jpg|left|200px]] | ||
'''Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator''' | {{Structure | ||
|PDB= 1ny9 |SIZE=350|CAPTION= <scene name='initialview01'>1ny9</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= tipA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans]) | |||
}} | |||
'''Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NY9 is a [ | 1NY9 is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12682015 12682015] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces lividans]] | [[Category: Streptomyces lividans]] | ||
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[[Category: globin like]] | [[Category: globin like]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:03:16 2008'' | ||
Revision as of 11:03, 20 March 2008
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| Gene: | tipA (Streptomyces lividans) | ||||||||||||
| 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
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