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2xpu

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Revision as of 08:19, 11 August 2016

TetR(D) in complex with anhydrotetracycline.

Structural highlights

2xpu is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	2xgc, 2xpw, 3zqg, 2x9d, 1bjz, 3zqh, 2trt, 2xpv, 2vkv, 1ork, 2xge, 1a6i, 2x6o, 2vke, 1qpi, 1du7, 2xgd, 2xrl, 2xpt, 2xb5, 2xps, 1bj0, 3zqf, 3zqi, 2tct, 1bjy
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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.

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^[1]

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

References

↑ Werten S, Dalm D, Palm GJ, Grimm CC, Hinrichs W. Tetracycline Repressor Allostery Does Not Depend on Divalent Metal Recognition. Biochemistry. 2014 Dec 9. PMID:25432019 doi:http://dx.doi.org/10.1021/bi5012805

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xpu"

@@ Line 1: / Line 1: @@
 ==TetR(D) in complex with anhydrotetracycline.==
 <StructureSection load='2xpu' size='340' side='right' caption='[[2xpu]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TDC:5A,6-ANHYDROTETRACYCLINE'>TDC</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xgc|2xgc]], [[2xpw|2xpw]], [[3zqg|3zqg]], [[2x9d|2x9d]], [[1bjz|1bjz]], [[3zqh|3zqh]], [[2trt|2trt]], [[2xpv|2xpv]], [[2vkv|2vkv]], [[1ork|1ork]], [[2xge|2xge]], [[1a6i|1a6i]], [[2x6o|2x6o]], [[2vke|2vke]], [[1qpi|1qpi]], [[1du7|1du7]], [[2xgd|2xgd]], [[2xrl|2xrl]], [[2xpt|2xpt]], [[2xb5|2xb5]], [[2xps|2xps]], [[1bj0|1bj0]], [[3zqf|3zqf]], [[3zqi|3zqi]], [[2tct|2tct]], [[1bjy|1bjy]]</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=2xpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xpu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xpu RCSB], [http://www.ebi.ac.uk/pdbsum/2xpu PDBsum]</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=2xpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xpu OCA], [http://pdbe.org/2xpu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xpu RCSB], [http://www.ebi.ac.uk/pdbsum/2xpu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xpu ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2xpu" style="background-color:#fffaf0;"></div>
 ==See Also==

2xpu

From Proteopedia

Revision as of 08:19, 11 August 2016

TetR(D) in complex with anhydrotetracycline.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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