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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]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<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/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965]. 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>
<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1exj|1exj]], [[1exi|1exi]], [[1jbg|1jbg]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tipA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 "Actinomyces lividans" Krasil'nikov et al. 1965])</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>
<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.  
[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.
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>
From MEDLINE&reg;/PubMed&reg;, 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, M G]]
[[Category: Streptomyces lividans]]
[[Category: Grzesiek, S]]
[[Category: Allan MG]]
[[Category: Kahmann, J D]]
[[Category: Grzesiek S]]
[[Category: Sass, H J]]
[[Category: Kahmann JD]]
[[Category: Seto, H]]
[[Category: Sass HJ]]
[[Category: Thompson, C J]]
[[Category: Seto H]]
[[Category: All alpha]]
[[Category: Thompson CJ]]
[[Category: Globin like]]
[[Category: Transcription]]

Revision as of 08:54, 10 April 2024

Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator

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