1ny9

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(New page: 200px<br /><applet load="1ny9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ny9" /> '''Antibiotic binding domain of a TipA-class mu...)
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[[Image:1ny9.jpg|left|200px]]<br /><applet load="1ny9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ny9" />
 
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'''Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator'''<br />
 
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==Overview==
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==Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator==
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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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<StructureSection load='1ny9' size='340' side='right'caption='[[1ny9]]' scene=''>
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== Structural highlights ==
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<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>
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</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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TIPA_STRLI TIPA_STRLI] Transcriptional activator. Is activated when bound to the antibiotic thiostrepton.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ny/1ny9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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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1NY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NY9 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12682015 12682015]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1ny9" style="background-color:#fffaf0;"></div>
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[[Category: Streptomyces lividans]]
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[[Category: Allan, M.G.]]
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[[Category: Grzesiek, S.]]
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[[Category: Kahmann, J.D.]]
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[[Category: Sass, H.J.]]
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[[Category: Seto, H.]]
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[[Category: Thompson, C.J.]]
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[[Category: all alpha]]
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[[Category: globin like]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:39:18 2007''
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==See Also==
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptomyces lividans]]
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[[Category: Allan MG]]
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[[Category: Grzesiek S]]
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[[Category: Kahmann JD]]
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[[Category: Sass HJ]]
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[[Category: Seto H]]
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[[Category: Thompson CJ]]

Current revision

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

PDB ID 1ny9

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