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| | ==Crystal structure of TsaR in complex with its effector p-toluenesulfonate== | | ==Crystal structure of TsaR in complex with its effector p-toluenesulfonate== |
| - | <StructureSection load='3fxu' size='340' side='right' caption='[[3fxu]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='3fxu' size='340' side='right'caption='[[3fxu]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fxu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11996 Atcc 11996]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FXU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fxu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FXU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=TSU:PARA-TOLUENE+SULFONATE'>TSU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fxq|3fxq]], [[3fxr|3fxr]], [[3fzj|3fzj]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=TSU:PARA-TOLUENE+SULFONATE'>TSU</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tsaR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=285 ATCC 11996])</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=3fxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fxu OCA], [https://pdbe.org/3fxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fxu RCSB], [https://www.ebi.ac.uk/pdbsum/3fxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fxu ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fxu OCA], [http://pdbe.org/3fxu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fxu RCSB], [http://www.ebi.ac.uk/pdbsum/3fxu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fxu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TSAR_COMTE TSAR_COMTE] Regulates expression of the tsaMBCD1 operon and of tsaT in response to p-toluenesulfonate (TSA). Acts by binding directly to the promoter region. Binding to the tsa promoter depends on TSA concentration.<ref>PMID:12676713</ref> <ref>PMID:13680097</ref> |
| | == 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: Atcc 11996]] | + | [[Category: Comamonas testosteroni]] |
| - | [[Category: Kertesz, M A]] | + | [[Category: Large Structures]] |
| - | [[Category: Kikhney, A]] | + | [[Category: Kertesz MA]] |
| - | [[Category: Monferrer, D]] | + | [[Category: Kikhney A]] |
| - | [[Category: Svergun, D]] | + | [[Category: Monferrer D]] |
| - | [[Category: Tralau, T]] | + | [[Category: Svergun D]] |
| - | [[Category: Uson, I]] | + | [[Category: Tralau T]] |
| - | [[Category: Dna-binding]]
| + | [[Category: Uson I]] |
| - | [[Category: Lttr]]
| + | |
| - | [[Category: Lysr-type]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| - | [[Category: Transcription regulator]]
| + | |
| - | [[Category: Transcriptional regulator]]
| + | |
| - | [[Category: Tsar]]
| + | |
| - | [[Category: Whth]]
| + | |
| Structural highlights
3fxu is a 2 chain structure with sequence from Comamonas testosteroni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.95Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
TSAR_COMTE Regulates expression of the tsaMBCD1 operon and of tsaT in response to p-toluenesulfonate (TSA). Acts by binding directly to the promoter region. Binding to the tsa promoter depends on TSA concentration.[1] [2]
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
LysR-type transcriptional regulators (LTTRs) constitute the largest family of regulators in prokaryotes. The full-length structures of the LTTR TsaR from Comamonas testosteroni T-2 and its complex with the natural inducer para-toluensulfonate have been characterized by X-ray diffraction. Both ligand-free and complexed forms reveal a dramatically different quaternary structure from that of CbnR from Ralstonia eutropha, or a putative LysR-type regulator from Pseudomonas aeruginosa, the only other determined full-length structures of tetrameric LTTRs. Although all three show a head-to-head tetrameric ring, TsaR displays an open conformation, whereas CbnR and PA01-PR present additional contacts in opposing C-terminal domains that close the ring. Such large differences may be due to a broader structural versatility than previously assumed or either, reflect the intrinsic flexibility of tetrameric LTTRs. On the grounds of the sliding dimer hypothesis of LTTR activation, we propose a structural model in which the closed structures could reflect the conformation of a ligand-free LTTR, whereas inducer binding would bring about local changes to disrupt the interface linking the two compact C-terminal domains. This could lead to a TsaR-like, open structure, where the pairs of recognition helices are closer to each other by more than 10 A.
Structural studies on the full-length LysR-type regulator TsaR from Comamonas testosteroni T-2 reveal a novel open conformation of the tetrameric LTTR fold.,Monferrer D, Tralau T, Kertesz MA, Dix I, Sola M, Uson I Mol Microbiol. 2010 Mar;75(5):1199-214. Epub 2010 Jan 5. PMID:20059681[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tralau T, Mampel J, Cook AM, Ruff J. Characterization of TsaR, an oxygen-sensitive LysR-type regulator for the degradation of p-toluenesulfonate in Comamonas testosteroni T-2. Appl Environ Microbiol. 2003 Apr;69(4):2298-305. PMID:12676713 doi:10.1128/AEM.69.4.2298-2305.2003
- ↑ Tralau T, Cook AM, Ruff J. An additional regulator, TsaQ, is involved with TsaR in regulation of transport during the degradation of p-toluenesulfonate in Comamonas testosteroni T-2. Arch Microbiol. 2003 Nov;180(5):319-26. PMID:13680097 doi:10.1007/s00203-003-0594-8
- ↑ Monferrer D, Tralau T, Kertesz MA, Dix I, Sola M, Uson I. Structural studies on the full-length LysR-type regulator TsaR from Comamonas testosteroni T-2 reveal a novel open conformation of the tetrameric LTTR fold. Mol Microbiol. 2010 Mar;75(5):1199-214. Epub 2010 Jan 5. PMID:20059681 doi:10.1111/j.1365-2958.2010.07043.x
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