1a6i: Difference between revisions

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-[[Image:1a6i.gif|left|200px]]<br /><applet load="1a6i" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1a6i, resolution 2.4&Aring;" />
-'''TET REPRESSOR, CLASS D VARIANT'''<br />
-==Overview==
+==TET REPRESSOR, CLASS D VARIANT==
-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.
+<StructureSection load='1a6i' size='340' side='right'caption='[[1a6i]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+</table>
+== Function ==
+[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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/1a6i_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==About this Structure==
+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>
-A6I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Known structural/functional Site: <scene name='pdbsite=TNE:Empty+Tetracycline+Binding+Tunnel'>TNE</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6I OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9642048 9642048]
+</div>
+<div class="pdbe-citations 1a6i" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Cordes, F.]]
+[[Category: Cordes F]]
-[[Category: Hillen, W.]]
+[[Category: Hillen W]]
-[[Category: Hinrichs, W.]]
+[[Category: Hinrichs W]]
-[[Category: Orth, P.]]
+[[Category: Orth P]]
-[[Category: Saenger, W.]]
+[[Category: Saenger W]]
-[[Category: Schnappinger, D.]]
+[[Category: Schnappinger D]]
-[[Category: dna-binding]]
-[[Category: repressor]]
-[[Category: transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:29:21 2008''