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[[Image:2jhe.png|left|200px]]
==N-TERMINAL DOMAIN OF TYRR TRANSCRIPTION FACTOR (RESIDUES 1 -190)==
<StructureSection load='2jhe' size='340' side='right' caption='[[2jhe]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
[[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]. <br>
<b>Activity:</b> <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><br>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jh/2jhe_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
== Publication Abstract from PubMed ==
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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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>
The line below this paragraph, containing "STRUCTURE_2jhe", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2jhe|  PDB=2jhe  |  SCENE=  }}


===N-TERMINAL DOMAIN OF TYRR TRANSCRIPTION FACTOR (RESIDUES 1 -190)===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
== References ==
 
<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_17222426}}, adds the Publication Abstract to the page
</StructureSection>
(as it appears on PubMed at http://www.pubmed.gov), where 17222426 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17222426}}
 
==About this Structure==
[[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].
 
==Reference==
<ref group="xtra">PMID:017222426</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Carr, P D.]]
[[Category: Carr, P D.]]

Revision as of 08:44, 30 April 2014

N-TERMINAL DOMAIN OF TYRR TRANSCRIPTION FACTOR (RESIDUES 1 -190)

2jhe, resolution 2.30Å

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