1ny9

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|ACTIVITY=
|ACTIVITY=
|GENE= tipA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans])
|GENE= tipA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans])
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|DOMAIN=
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|RELATEDENTRY=[[1exj|1EXJ]], [[1exi|1EXI]], [[1jbg|1JBG]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ny9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ny9 OCA], [http://www.ebi.ac.uk/pdbsum/1ny9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ny9 RCSB]</span>
}}
}}
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[[Category: globin like]]
[[Category: globin like]]
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Revision as of 19:37, 30 March 2008


PDB ID 1ny9

Drag the structure with the mouse to rotate
Gene: tipA (Streptomyces lividans)
Related: 1EXJ, 1EXI, 1JBG


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

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