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| - | ==TETR(D) IN COMPLEX WITH ANHYDROTETRACYCLINE AND POTASSIUM==
| + | #REDIRECT [[4d7n]] This PDB entry is obsolete and replaced by 4d7n |
| - | <StructureSection load='2xpt' size='340' side='right' caption='[[2xpt]], [[Resolution|resolution]] 1.89Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[2xpt]] 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=2XPT OCA]. <br>
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| - | </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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TDC:5A,6-ANHYDROTETRACYCLINE'>TDC</scene><br>
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| - | <tr><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]], [[2xpu|2xpu]], [[2xb5|2xb5]], [[2xps|2xps]], [[3zqf|3zqf]], [[3zqi|3zqi]], [[1bj0|1bj0]], [[1bjy|1bjy]], [[2tct|2tct]]</td></tr>
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| - | <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>
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| - | <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=2xpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xpt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xpt RCSB], [http://www.ebi.ac.uk/pdbsum/2xpt PDBsum]</span></td></tr>
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| - | <table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Escherichia coli]]
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| - | [[Category: Dalm, D.]]
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| - | [[Category: Hinrichs, W.]]
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| - | [[Category: Palm, G J.]]
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| - | [[Category: Helix-turn-helix]]
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| - | [[Category: Metal coordination]]
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| - | [[Category: Transcription]]
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| - | [[Category: Transcription regulator]]
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