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==TETR(D) IN COMPLEX WITH OXYTETRACYCLINE AND MAGNESIUM.==
 
<StructureSection load='2xpw' size='340' side='right' caption='[[2xpw]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
==TetR(D) in complex with oxytetracycline and magnesium.==
<StructureSection load='2xpw' size='340' side='right'caption='[[2xpw]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2xpw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XPW OCA]. <br>
<table><tr><td colspan='2'>[[2xpw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XPW FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OTC:OXYTETRACYCLINE'>OTC</scene><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]] 1.44&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xgc|2xgc]], [[1bjz|1bjz]], [[3zqg|3zqg]], [[2x9d|2x9d]], [[3zqh|3zqh]], [[2trt|2trt]], [[2xpv|2xpv]], [[2vkv|2vkv]], [[1ork|1ork]], [[2xge|2xge]], [[2x6o|2x6o]], [[1a6i|1a6i]], [[1qpi|1qpi]], [[2vke|2vke]], [[2xgd|2xgd]], [[1du7|1du7]], [[2xrl|2xrl]], [[2xpt|2xpt]], [[2xpu|2xpu]], [[2xb5|2xb5]], [[3zqi|3zqi]], [[3zqf|3zqf]], [[2xps|2xps]], [[1bj0|1bj0]], [[2tct|2tct]], [[1bjy|1bjy]]</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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OTC:OXYTETRACYCLINE'>OTC</scene></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2xpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xpw OCA], [https://pdbe.org/2xpw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xpw RCSB], [https://www.ebi.ac.uk/pdbsum/2xpw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xpw ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xpw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xpw RCSB], [http://www.ebi.ac.uk/pdbsum/2xpw PDBsum]</span></td></tr>
</table>
<table>
== Function ==
<div style="background-color:#fffaf0;">
[https://www.uniprot.org/uniprot/TETR4_ECOLX 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 ==
The most frequently occurring resistance of Gram-negative bacteria against tetracyclines is triggered by drug recognition of the Tet repressor. This causes dissociation of the repressor-operator DNA complex and enables expression of the resistance protein TetA, which is responsible for active efflux of tetracycline. The 2.5 angstrom resolution crystal structure of the homodimeric Tet repressor complexed with tetracycline-magnesium reveals detailed drug recognition. The orientation of the operator-binding helix-turn-helix motifs of the repressor is inverted in comparison with other DNA binding proteins. The repressor-drug complex is unable to interact with DNA because the separation of the DNA binding motifs is 5 angstroms wider than usually observed.
 
Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance.,Hinrichs W, Kisker C, Duvel M, Muller A, Tovar K, Hillen W, Saenger W Science. 1994 Apr 15;264(5157):418-20. PMID:8153629<ref>PMID:8153629</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Dalm, D.]]
[[Category: Large Structures]]
[[Category: Hinrichs, W.]]
[[Category: Dalm D]]
[[Category: Palm, G J.]]
[[Category: Hinrichs W]]
[[Category: Proft, J.]]
[[Category: Palm GJ]]
[[Category: Helix-turn-helix]]
[[Category: Proft J]]
[[Category: Metal coordination]]
[[Category: Transcription]]
[[Category: Transcription regulator]]

Latest revision as of 08:02, 23 August 2023

TetR(D) in complex with oxytetracycline and magnesium.

2xpw, resolution 1.44Å

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