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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 [http://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 [http://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 ([http://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'>[http://proteopedia.org/fgij/fg.htm?mol=1ny9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ny9 OCA], [http://pdbe.org/1ny9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ny9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ny9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ny9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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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| | __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]]
| + | |
| Structural highlights
Function
TIPA_STRLI Transcriptional activator. Is activated when bound to the antibiotic thiostrepton.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kahmann JD, Sass HJ, Allan MG, Seto H, Thompson CJ, Grzesiek S. Structural basis for antibiotic recognition by the TipA class of multidrug-resistance transcriptional regulators. EMBO J. 2003 Apr 15;22(8):1824-34. PMID:12682015 doi:10.1093/emboj/cdg181
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