2jhe

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[[Image:2jhe.png|left|200px]]
 
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==N-terminal domain of TyrR transcription factor (residues 1 - 190)==
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The line below this paragraph, containing "STRUCTURE_2jhe", creates the "Structure Box" on the page.
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<StructureSection load='2jhe' size='340' side='right'caption='[[2jhe]], [[Resolution|resolution]] 2.30&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'>[[2jhe]] is a 4 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=2JHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JHE FirstGlance]. <br>
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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]] 2.3&#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=AE3:2-(2-ETHOXYETHOXY)ETHANOL'>AE3</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2jhe| PDB=2jhe | 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=2jhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jhe OCA], [https://pdbe.org/2jhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jhe RCSB], [https://www.ebi.ac.uk/pdbsum/2jhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jhe ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TYRR_ECOLI TYRR_ECOLI] Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP gene have been observed at high phenylalanine concentrations.
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jh/2jhe_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=2jhe 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 structure of the N-terminal domain of TyrR has been solved to a resolution of 2.3 A. It reveals a modular protein containing an ACT domain, a connecting helix, a PAS domain and a C-terminal helix. Two dimers are present in the asymmetric unit with one monomer of each pair exhibiting a large rigid-body movement that results in a hinging around residue 74 of approximately 50 degrees . The structure of the dimer is discussed with reference to other transcription regulator proteins. Putative binding sites are identified for the aromatic amino acid cofactors.
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===N-TERMINAL DOMAIN OF TYRR TRANSCRIPTION FACTOR (RESIDUES 1 -190)===
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Crystal structure of the N-terminal domain of the TyrR transcription factor responsible for gene regulation of aromatic amino acid biosynthesis and transport in Escherichia coli K12.,Verger D, Carr PD, Kwok T, Ollis DL J Mol Biol. 2007 Mar 16;367(1):102-12. Epub 2006 Dec 12. PMID:17222426<ref>PMID:17222426</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 2jhe" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17222426 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17222426}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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[[2jhe]] is a 4 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=2JHE OCA].
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[[Category: Large Structures]]
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[[Category: Carr PD]]
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==Reference==
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[[Category: Kwok T]]
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<ref group="xtra">PMID:017222426</ref><references group="xtra"/>
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[[Category: Ollis DL]]
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[[Category: Escherichia coli]]
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[[Category: Verger D]]
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[[Category: Carr, P D.]]
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[[Category: Kwok, T.]]
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[[Category: Ollis, D L.]]
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[[Category: Verger, D.]]
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[[Category: Activator]]
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[[Category: Aromatic hydrocarbons catabolism]]
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[[Category: Atp-binding]]
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[[Category: Dna-binding]]
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[[Category: Nucleotide-binding]]
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[[Category: Repressor]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Two-component regulatory system]]
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[[Category: Tyrr protein]]
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Current revision

N-terminal domain of TyrR transcription factor (residues 1 - 190)

PDB ID 2jhe

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