4d7n: Difference between revisions

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~~'''Unreleased structure'''~~

~~The~~ entry 4d7n is ~~ON HOLD until sometime~~ in the ~~future~~

==TetR(D) in complex with anhydrotetracycline and potassium==

== Structural highlights ==

<table><tr><td colspan='2'>[[4d7n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2xpt 2xpt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D7N FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76Å</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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TDC:5A,6-ANHYDROTETRACYCLINE'>TDC</scene></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=4d7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d7n OCA], [https://pdbe.org/4d7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d7n RCSB], [https://www.ebi.ac.uk/pdbsum/4d7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d7n ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Genes that render bacteria resistant to tetracycline-derived antibiotics are tightly regulated by repressors of the TetR family. In their physiologically relevant, magnesium-complexed form, tetracyclines induce allosteric rearrangements in the TetR homodimer, leading to its release from the promoter and derepression of transcription. According to earlier crystallographic work, recognition of the tetracycline-associated magnesium ion by TetR is crucial and triggers the allosteric cascade. Nevertheless, the derivative 5a,6-anhydrotetracycline, which shows an increased affinity for TetR, causes promoter release even in the absence of magnesium. To resolve this paradox, it has been proposed that metal-free 5a,6-anhydrotetracycline acts via an exceptional, conformationally different induction mode that circumvents the normal magnesium requirement. We have tested this hypothesis by determining crystal structures of TetR-5a,6-anhydrotetracycline complexes in the presence of magnesium, ethylenediaminetetraacetic acid, or high concentrations of potassium. Analysis of these three structures reveals that, irrespective of the metal, the effects of 5a,6-anhydrotetracycline binding are indistinguishable from those of canonical induction by other tetracyclines. Together with a close scrutiny of the earlier evidence of a metal-triggered mechanism, these results demonstrate that magnesium recognition per se is not a prerequisite for tetracycline repressor allostery.

~~Authors:~~ Werten, S., Dalm, D., Palm, ~~G.J.~~, Hinrichs, W.

Tetracycline Repressor Allostery Does Not Depend on Divalent Metal Recognition.,Werten S, Dalm D, Palm GJ, Grimm CC, Hinrichs W Biochemistry. 2014 Dec 9. PMID:25432019<ref>PMID:25432019</ref>

~~Description~~: ~~TetR(~~D~~) in complex with anhydrotetracycline and potassium~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Escherichia coli]]

[[Category: Large Structures]]

[[Category: Dalm D]]

[[Category: Hinrichs W]]

[[Category: Palm GJ]]

[[Category: Werten S]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4d7n is ON HOLD  until sometime in the future
+==TetR(D) in complex with anhydrotetracycline and potassium==
+<StructureSection load='4d7n' size='340' side='right'caption='[[4d7n]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4d7n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2xpt 2xpt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D7N FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TDC:5A,6-ANHYDROTETRACYCLINE'>TDC</scene></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=4d7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d7n OCA], [https://pdbe.org/4d7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d7n RCSB], [https://www.ebi.ac.uk/pdbsum/4d7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d7n ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Genes that render bacteria resistant to tetracycline-derived antibiotics are tightly regulated by repressors of the TetR family. In their physiologically relevant, magnesium-complexed form, tetracyclines induce allosteric rearrangements in the TetR homodimer, leading to its release from the promoter and derepression of transcription. According to earlier crystallographic work, recognition of the tetracycline-associated magnesium ion by TetR is crucial and triggers the allosteric cascade. Nevertheless, the derivative 5a,6-anhydrotetracycline, which shows an increased affinity for TetR, causes promoter release even in the absence of magnesium. To resolve this paradox, it has been proposed that metal-free 5a,6-anhydrotetracycline acts via an exceptional, conformationally different induction mode that circumvents the normal magnesium requirement. We have tested this hypothesis by determining crystal structures of TetR-5a,6-anhydrotetracycline complexes in the presence of magnesium, ethylenediaminetetraacetic acid, or high concentrations of potassium. Analysis of these three structures reveals that, irrespective of the metal, the effects of 5a,6-anhydrotetracycline binding are indistinguishable from those of canonical induction by other tetracyclines. Together with a close scrutiny of the earlier evidence of a metal-triggered mechanism, these results demonstrate that magnesium recognition per se is not a prerequisite for tetracycline repressor allostery.
-Authors: Werten, S., Dalm, D., Palm, G.J., Hinrichs, W.
+Tetracycline Repressor Allostery Does Not Depend on Divalent Metal Recognition.,Werten S, Dalm D, Palm GJ, Grimm CC, Hinrichs W Biochemistry. 2014 Dec 9. PMID:25432019<ref>PMID:25432019</ref>
-Description: TetR(D) in complex with anhydrotetracycline and potassium
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4d7n" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
+[[Category: Dalm D]]
+[[Category: Hinrichs W]]
+[[Category: Palm GJ]]
+[[Category: Werten S]]