3fxq: Difference between revisions

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<StructureSection load='3fxq' size='340' side='right'caption='[[3fxq]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='3fxq' size='340' side='right'caption='[[3fxq]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3fxq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_11996 Atcc 11996]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FXQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3fxq]] 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=3FXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FXQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.85&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fxr|3fxr]], [[3fxu|3fxu]], [[3fzj|3fzj]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tsaR ([https://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=3fxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fxq OCA], [https://pdbe.org/3fxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fxq RCSB], [https://www.ebi.ac.uk/pdbsum/3fxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fxq 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=3fxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fxq OCA], [https://pdbe.org/3fxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fxq RCSB], [https://www.ebi.ac.uk/pdbsum/3fxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fxq 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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</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=3fxq 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=3fxq ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:20059681</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3fxq" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 11996]]
[[Category: Comamonas testosteroni]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kertesz, M A]]
[[Category: Kertesz MA]]
[[Category: Kikhney, A]]
[[Category: Kikhney A]]
[[Category: Monferrer, D]]
[[Category: Monferrer D]]
[[Category: Svergun, D]]
[[Category: Svergun D]]
[[Category: Tralau, T]]
[[Category: Tralau T]]
[[Category: Uson, I]]
[[Category: Uson I]]
[[Category: Dna-binding]]
[[Category: Lttr]]
[[Category: Lysr-type]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
[[Category: Transcription regulator]]
[[Category: Transcriptional regulator]]
[[Category: Tsar]]
[[Category: Whth]]

Latest revision as of 11:25, 20 March 2024

Crystal structure of the LysR-type transcriptional regulator TsaRCrystal structure of the LysR-type transcriptional regulator TsaR

Structural highlights

3fxq 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 1.85Å
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.

References

  1. ↑ 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
  2. ↑ 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

3fxq, resolution 1.85Å

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