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4aux

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Current revision (11:36, 20 December 2023) (edit) (undo)
 
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<StructureSection load='4aux' size='340' side='right'caption='[[4aux]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='4aux' size='340' side='right'caption='[[4aux]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4aux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AUX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4aux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AUX FirstGlance]. <br>
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</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=XTC:(4S,4AS,5AR,12AS)-4-(DIMETHYLAMINO)-3,10,12,12A-TETRAHYDROXY-9-NITRO-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE'>XTC</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a6i|1a6i]], [[1bj0|1bj0]], [[1bjy|1bjy]], [[1bjz|1bjz]], [[1du7|1du7]], [[1ork|1ork]], [[1qpi|1qpi]], [[2tct|2tct]], [[2trt|2trt]], [[2vke|2vke]], [[2vkv|2vkv]], [[2x6o|2x6o]], [[2x9d|2x9d]], [[2xb5|2xb5]], [[2xgc|2xgc]], [[2xgd|2xgd]], [[2xge|2xge]], [[2xps|2xps]], [[2xpt|2xpt]], [[2xpu|2xpu]], [[2xpv|2xpv]], [[2xpw|2xpw]], [[2xrl|2xrl]], [[3zqf|3zqf]], [[3zqg|3zqg]], [[3zqh|3zqh]], [[3zqi|3zqi]], [[4abz|4abz]]</div></td></tr>
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<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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=XTC:(4S,4AS,5AR,12AS)-4-(DIMETHYLAMINO)-3,10,12,12A-TETRAHYDROXY-9-NITRO-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE'>XTC</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=4aux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aux OCA], [https://pdbe.org/4aux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aux RCSB], [https://www.ebi.ac.uk/pdbsum/4aux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aux 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=4aux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aux OCA], [https://pdbe.org/4aux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aux RCSB], [https://www.ebi.ac.uk/pdbsum/4aux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aux ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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.
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4aux" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hinrichs, W]]
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[[Category: Hinrichs W]]
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[[Category: Orth, P]]
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[[Category: Orth P]]
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[[Category: Saenger, W]]
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[[Category: Saenger W]]
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[[Category: Antibiotic]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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Current revision

Tet repressor class D in complex with 9-nitrotetracycline

PDB ID 4aux

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