2pbx: Difference between revisions

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[[Image:2pbx.jpg|left|200px]]


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==Vibrio cholerae HapR==
The line below this paragraph, containing "STRUCTURE_2pbx", creates the "Structure Box" on the page.
<StructureSection load='2pbx' size='340' side='right'caption='[[2pbx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2pbx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_2740-80 Vibrio cholerae 2740-80]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PBX FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#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=2pbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pbx OCA], [https://pdbe.org/2pbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pbx RCSB], [https://www.ebi.ac.uk/pdbsum/2pbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pbx ProSAT]</span></td></tr>
{{STRUCTURE_2pbx| PDB=2pbx  | SCENE= }}
</table>
 
== Evolutionary Conservation ==
'''Vibrio cholerae HapR'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pb/2pbx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2pbx ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Quorum sensing in Vibrio cholerae involves signaling between two-component sensor protein kinases and the response regulator LuxO to control the expression of the master regulator HapR. HapR, in turn, plays a central role in regulating a number of important processes, such as virulence gene expression and biofilm formation. We have determined the crystal structure of HapR to 2.2-A resolution. Its structure reveals a dimeric, two-domain molecule with an all-helical structure that is strongly conserved with members of the TetR family of transcriptional regulators. The N-terminal DNA-binding domain contains a helix-turn-helix DNA-binding motif and alteration of certain residues in this domain completely abolishes the ability of HapR to bind to DNA, alleviating repression of both virulence gene expression and biofilm formation. The C-terminal dimerization domain contains a unique solvent accessible tunnel connected to an amphipathic cavity, which by analogy with other TetR regulators, may serve as a binding pocket for an as-yet-unidentified ligand.
Quorum sensing in Vibrio cholerae involves signaling between two-component sensor protein kinases and the response regulator LuxO to control the expression of the master regulator HapR. HapR, in turn, plays a central role in regulating a number of important processes, such as virulence gene expression and biofilm formation. We have determined the crystal structure of HapR to 2.2-A resolution. Its structure reveals a dimeric, two-domain molecule with an all-helical structure that is strongly conserved with members of the TetR family of transcriptional regulators. The N-terminal DNA-binding domain contains a helix-turn-helix DNA-binding motif and alteration of certain residues in this domain completely abolishes the ability of HapR to bind to DNA, alleviating repression of both virulence gene expression and biofilm formation. The C-terminal dimerization domain contains a unique solvent accessible tunnel connected to an amphipathic cavity, which by analogy with other TetR regulators, may serve as a binding pocket for an as-yet-unidentified ligand.


==About this Structure==
Crystal structure of the Vibrio cholerae quorum-sensing regulatory protein HapR.,De Silva RS, Kovacikova G, Lin W, Taylor RK, Skorupski K, Kull FJ J Bacteriol. 2007 Aug;189(15):5683-91. Epub 2007 May 25. PMID:17526705<ref>PMID:17526705</ref>
2PBX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBX OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of the Vibrio cholerae quorum-sensing regulatory protein HapR., De Silva RS, Kovacikova G, Lin W, Taylor RK, Skorupski K, Kull FJ, J Bacteriol. 2007 Aug;189(15):5683-91. Epub 2007 May 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17526705 17526705]
</div>
[[Category: Bacteria]]
<div class="pdbe-citations 2pbx" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: DeSilva, R S.]]
<references/>
[[Category: Kovacikova, G.]]
__TOC__
[[Category: Kull, F J.]]
</StructureSection>
[[Category: Lin, W.]]
[[Category: Large Structures]]
[[Category: Skorupski, K.]]
[[Category: Vibrio cholerae 2740-80]]
[[Category: Taylor, R K.]]
[[Category: DeSilva RS]]
[[Category: Dna-binding]]
[[Category: Kovacikova G]]
[[Category: Protease]]
[[Category: Kull FJ]]
[[Category: Quorum sensing]]
[[Category: Lin W]]
[[Category: Tetr family]]
[[Category: Skorupski K]]
[[Category: Transcription factor]]
[[Category: Taylor RK]]
[[Category: Transcription regulation]]
[[Category: Vibrio cholerae]]
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