This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ny9
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1ny9.jpg|left|200px]] | [[Image:1ny9.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1ny9", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1ny9| PDB=1ny9 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator''' | '''Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator''' | ||
| Line 31: | Line 28: | ||
[[Category: Seto, H.]] | [[Category: Seto, H.]] | ||
[[Category: Thompson, C J.]] | [[Category: Thompson, C J.]] | ||
| - | [[Category: | + | [[Category: All alpha]] |
| - | [[Category: | + | [[Category: Globin like]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:07:47 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:07, 3 May 2008
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 Sat May 3 03:07:47 2008
