2vke

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{{Seed}}
 
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[[Image:2vke.png|left|200px]]
 
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==Tet repressor class D complexed with cobalt and tetracycline==
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The line below this paragraph, containing "STRUCTURE_2vke", creates the "Structure Box" on the page.
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<StructureSection load='2vke' size='340' side='right'caption='[[2vke]], [[Resolution|resolution]] 1.62&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'>[[2vke]] 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=2VKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VKE 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]] 1.62&#8491;</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=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=TAC:TETRACYCLINE'>TAC</scene></td></tr>
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{{STRUCTURE_2vke| PDB=2vke | SCENE= }}
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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=2vke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vke OCA], [https://pdbe.org/2vke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vke RCSB], [https://www.ebi.ac.uk/pdbsum/2vke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vke ProSAT]</span></td></tr>
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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/vk/2vke_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=2vke 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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Tetracyclines coordinate metal(II) ions under physiological conditions forming chelate complexes with their ketoenolate moiety at rings B and C. These metal(II) complexes are the biologically relevant molecules conferring the antibiotic character of the drug by inhibiting ribosomal protein biosynthesis in prokaryotes. The Tet repressor, TetR, is the molecular switch for tetracycline resistance determinants in gram-negative bacteria. TetR controls transcription of a gene encoding the integral membrane protein TetA, which mediates active efflux of a tetracycline-metal(II) cation, [MeTc](+), by equimolar antiport with a proton. We evaluated distinct characteristics of the metal binding by crystal structure determination of TetR/[MeTc](+) complexes and of association equilibrium constants of [MeTc](+) and TetR/[MeTc](+) complexes. Various divalent metal ions bind to the same octahedral coordination site, defined by a histidine side chain of TetR, the tetracycline, and three water molecules. Whereas association constants for [MeTc](+) vary within 3 orders of magnitude, association of the [MeTc](+) cation to TetR is very similar for all measured divalent metals. Taking intracellular cation concentrations into account, it is evident that no other metal ion can compete with Mg(2+) for TetR/[MeTc](+) complex formation.
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===TET REPRESSOR CLASS D COMPLEXED WITH COBALT AND TETRACYCLINE===
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Specific binding of divalent metal ions to tetracycline and to the Tet repressor/tetracycline complex.,Palm GJ, Lederer T, Orth P, Saenger W, Takahashi M, Hillen W, Hinrichs W J Biol Inorg Chem. 2008 Jun 12;. PMID:18548290<ref>PMID:18548290</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 2vke" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18548290}}, adds the Publication Abstract to the page
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*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18548290 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18548290}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2VKE 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=2VKE OCA].
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==Reference==
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Specific binding of divalent metal ions to tetracycline and to the Tet repressor/tetracycline complex., Palm GJ, Lederer T, Orth P, Saenger W, Takahashi M, Hillen W, Hinrichs W, J Biol Inorg Chem. 2008 Jun 12;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18548290 18548290]
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[[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: Hinrichs, W.]]
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[[Category: Hinrichs W]]
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[[Category: Palm, G J.]]
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[[Category: Palm GJ]]
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[[Category: Antibiotic resistance]]
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[[Category: Cobalt]]
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[[Category: Dna-binding]]
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[[Category: Helix-turn-helix]]
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[[Category: Magnesium]]
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[[Category: Metal coordination]]
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[[Category: Metal-binding]]
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[[Category: Plasmid]]
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[[Category: Repressor]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Transcription regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:27:35 2008''
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Current revision

Tet repressor class D complexed with cobalt and tetracycline

PDB ID 2vke

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