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1a6i

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[[Image:1a6i.gif|left|200px]]
 
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==TET REPRESSOR, CLASS D VARIANT==
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The line below this paragraph, containing "STRUCTURE_1a6i", creates the "Structure Box" on the page.
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<StructureSection load='1a6i' size='340' side='right'caption='[[1a6i]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1a6i]] 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=1A6I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A6I FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6i OCA], [https://pdbe.org/1a6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a6i RCSB], [https://www.ebi.ac.uk/pdbsum/1a6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a6i ProSAT]</span></td></tr>
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{{STRUCTURE_1a6i| PDB=1a6i | SCENE= }}
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</table>
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== Function ==
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/1a6i_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a6i ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The X-ray crystal structure analysis of inducer-free Tet repressor, TetR, at 2.4 A resolution identifies one of two openings of the tunnel-like binding site as the entrance for the inducer tetracycline-Mg2+, [Mg Tc]+. Recognition and binding of the inducer unleashes conformational changes leading to the induced state of TetR. In the first step, the C-terminal turn of alpha-helix 6 unwinds, thereby altering the orientation of alpha-helix 4. This different orientation of alpha-helix 4 is stabilized by a series of hydrogen bonds mediated through a chain of eight water molecules. The alpha-helix 4 connects the DNA-binding domain (alpha-helices 1 to 3) to the rigid TetR core, and thus regulates gene expression through its respective orientations.
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'''TET REPRESSOR, CLASS D VARIANT'''
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Conformational changes of the Tet repressor induced by tetracycline trapping.,Orth P, Cordes F, Schnappinger D, Hillen W, Saenger W, Hinrichs W J Mol Biol. 1998 Jun 5;279(2):439-47. PMID:9642048<ref>PMID:9642048</ref>
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==Overview==
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The X-ray crystal structure analysis of inducer-free Tet repressor, TetR, at 2.4 A resolution identifies one of two openings of the tunnel-like binding site as the entrance for the inducer tetracycline-Mg2+, [Mg Tc]+. Recognition and binding of the inducer unleashes conformational changes leading to the induced state of TetR. In the first step, the C-terminal turn of alpha-helix 6 unwinds, thereby altering the orientation of alpha-helix 4. This different orientation of alpha-helix 4 is stabilized by a series of hydrogen bonds mediated through a chain of eight water molecules. The alpha-helix 4 connects the DNA-binding domain (alpha-helices 1 to 3) to the rigid TetR core, and thus regulates gene expression through its respective orientations.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1A6I is a [[Single protein]] structure of 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=1A6I OCA].
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</div>
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<div class="pdbe-citations 1a6i" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Conformational changes of the Tet repressor induced by tetracycline trapping., Orth P, Cordes F, Schnappinger D, Hillen W, Saenger W, Hinrichs W, J Mol Biol. 1998 Jun 5;279(2):439-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9642048 9642048]
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*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cordes, F.]]
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[[Category: Cordes F]]
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[[Category: Hillen, W.]]
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[[Category: Hillen W]]
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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: Schnappinger, D.]]
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[[Category: Schnappinger D]]
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[[Category: Dna-binding]]
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[[Category: Repressor]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:53:22 2008''
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Current revision

TET REPRESSOR, CLASS D VARIANT

PDB ID 1a6i

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