6fpl: Difference between revisions
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<StructureSection load='6fpl' size='340' side='right'caption='[[6fpl]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='6fpl' size='340' side='right'caption='[[6fpl]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6fpl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FPL FirstGlance]. <br> | <table><tr><td colspan='2'>[[6fpl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FPL 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TAC:TETRACYCLINE'>TAC</scene></td></tr> | </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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TAC:TETRACYCLINE'>TAC</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2trt|2trt]], [[2tct|2tct]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2trt|2trt]], [[2tct|2tct]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tetR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=6fpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fpl OCA], [http://pdbe.org/6fpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fpl RCSB], [http://www.ebi.ac.uk/pdbsum/6fpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fpl 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=6fpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fpl OCA], [http://pdbe.org/6fpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fpl RCSB], [http://www.ebi.ac.uk/pdbsum/6fpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fpl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Allosteric regulation of the Tet repressor (TetR) homodimer relies on tetracycline binding that abolishes the affinity for the DNA operator. Previously, interpretation of circular dichroism data called for unfolding of the alpha-helical DNA-binding domains in absence of binding to DNA or tetracycline. Our small angle X-ray scattering of TetR(D) in solution contradicts this unfolding as a physiological process. Instead, in the core domain crystal structures analyses show increased immobilisation of helix alpha9 and two C-terminal turns of helix alpha8 upon tetracycline binding. Tetracycline complexes of TetR(D) and four single-site alanine variants were characterised by isothermal titration calorimetry, fluorescence titration, X-ray crystal structures, and melting curves. Five crystal structures confirm that Thr103 is a key residue for the allosteric events of induction, with the T103A variant lacking induction by any tetracycline. The T103A variant shows anti-cooperative inducer binding, and a melting curve of the tetracycline complex different to TetR(D) and other variants. For the N82A variant inducer binding is clearly anti-cooperative but triggers the induced conformation. | |||
Thermodynamics, cooperativity and stability of the tetracycline repressor (TetR) upon tetracycline binding.,Palm GJ, Buchholz I, Werten S, Girbardt B, Berndt L, Delcea M, Hinrichs W Biochim Biophys Acta Proteins Proteom. 2020 Feb 27;1868(6):140404. doi:, 10.1016/j.bbapap.2020.140404. PMID:32114262<ref>PMID:32114262</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 6fpl" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6fpl" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Berndt, L]] | [[Category: Berndt, L]] | ||
Latest revision as of 13:11, 18 March 2020
TETR(D) E147A MUTANT IN COMPLEX WITH TETRACYCLINE AND MAGNESIUMTETR(D) E147A MUTANT IN COMPLEX WITH TETRACYCLINE AND MAGNESIUM
Structural highlights
Function[TETR4_ECOLX] TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites. Publication Abstract from PubMedAllosteric regulation of the Tet repressor (TetR) homodimer relies on tetracycline binding that abolishes the affinity for the DNA operator. Previously, interpretation of circular dichroism data called for unfolding of the alpha-helical DNA-binding domains in absence of binding to DNA or tetracycline. Our small angle X-ray scattering of TetR(D) in solution contradicts this unfolding as a physiological process. Instead, in the core domain crystal structures analyses show increased immobilisation of helix alpha9 and two C-terminal turns of helix alpha8 upon tetracycline binding. Tetracycline complexes of TetR(D) and four single-site alanine variants were characterised by isothermal titration calorimetry, fluorescence titration, X-ray crystal structures, and melting curves. Five crystal structures confirm that Thr103 is a key residue for the allosteric events of induction, with the T103A variant lacking induction by any tetracycline. The T103A variant shows anti-cooperative inducer binding, and a melting curve of the tetracycline complex different to TetR(D) and other variants. For the N82A variant inducer binding is clearly anti-cooperative but triggers the induced conformation. Thermodynamics, cooperativity and stability of the tetracycline repressor (TetR) upon tetracycline binding.,Palm GJ, Buchholz I, Werten S, Girbardt B, Berndt L, Delcea M, Hinrichs W Biochim Biophys Acta Proteins Proteom. 2020 Feb 27;1868(6):140404. doi:, 10.1016/j.bbapap.2020.140404. PMID:32114262[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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