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1ny9
From Proteopedia
(Difference between revisions)
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==Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator== | ==Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator== | ||
| - | <StructureSection load='1ny9' size='340' side='right'caption='[[1ny9 | + | <StructureSection load='1ny9' size='340' side='right'caption='[[1ny9]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ny9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ny9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NY9 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ny9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ny9 OCA], [https://pdbe.org/1ny9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ny9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ny9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ny9 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ny9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ny9 OCA], [https://pdbe.org/1ny9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ny9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ny9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ny9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/TIPA_STRLI TIPA_STRLI] Transcriptional activator. Is activated when bound to the antibiotic thiostrepton. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ny9 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ny9 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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<ref>PMID:12682015</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1ny9" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Actinomyces lividans krasil'nikov et al. 1965]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Allan | + | [[Category: Streptomyces lividans]] |
| - | [[Category: Grzesiek | + | [[Category: Allan MG]] |
| - | [[Category: Kahmann | + | [[Category: Grzesiek S]] |
| - | [[Category: Sass | + | [[Category: Kahmann JD]] |
| - | [[Category: Seto | + | [[Category: Sass HJ]] |
| - | [[Category: Thompson | + | [[Category: Seto H]] |
| - | + | [[Category: Thompson CJ]] | |
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Revision as of 08:54, 10 April 2024
Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator
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