2bgc: Difference between revisions

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{{Seed}}
[[Image:2bgc.png|left|200px]]


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==PrfA-G145S, a constitutive active mutant of the Transcriptional Regulator In L.monocytogenes==
The line below this paragraph, containing "STRUCTURE_2bgc", creates the "Structure Box" on the page.
<StructureSection load='2bgc' size='340' side='right'caption='[[2bgc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2bgc]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BGC 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]] 2.3&#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=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=PR3:S,S-PROPYLTHIOCYSTEINE'>PR3</scene></td></tr>
{{STRUCTURE_2bgc|  PDB=2bgc  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bgc OCA], [https://pdbe.org/2bgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bgc RCSB], [https://www.ebi.ac.uk/pdbsum/2bgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bgc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRFA_LISMO PRFA_LISMO] Positively regulates expression of listeriolysin, of 1-phosphadidylinositol phosphodiesterase (PI-PLC) and other virulence factors.
== 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/bg/2bgc_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=2bgc ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Listeria monocytogenes, a Gram-positive, facultative intracellular human pathogen, causes systemic infections with high mortality rate. The majority of the known pathogenicity factors of L. monocytogenes is regulated by a single transcription factor, PrfA. Hyperhaemolytic laboratory strains of L. monocytogenes express the constitutively active mutant PrfA(G145S) inducing virulence gene overexpression independent of environmental conditions. PrfA belongs to the Crp/Fnr family of transcription factors generally activated by a small effector, such as cAMP or O(2). We present the crystal structures of wild-type PrfA, the first Gram-positive member of the Crp/Fnr family, and of the constitutively active mutant PrfA(G145S). Cap (Crp) has previously been described exclusively in the cAMP-induced (DNA-free and -bound) conformation. By contrast, the PrfA structures present views both of the non-induced state and of the mutationally activated form. The low DNA-binding affinity of wild-type PrfA is supported both structurally (partly disordered helix-turn-helix motif, overall geometry of the HTH alpha-helices deviates from Cap) and by surface plasmon resonance analyses (K(D) = 0.9 microM). In PrfA(G145S) the HTH motifs dramatically rearrange to adopt a conformation comparable to cAMP-induced Cap and hence favourable for DNA binding, supported by a DNA-binding affinity of 50 nM. Finally, the hypothesis that wild-type PrfA, like other Crp/Fnr family members, may require an as yet unidentified cofactor for activation is supported by the presence of a distinct tunnel in PrfA, located at the interface of the beta-barrel and the DNA-binding domain.


===PRFA-G145S, A CONSTITUTIVE ACTIVE MUTANT OF THE TRANSCRIPTIONAL REGULATOR IN L.MONOCYTOGENES===
The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif.,Eiting M, Hageluken G, Schubert WD, Heinz DW Mol Microbiol. 2005 Apr;56(2):433-46. PMID:15813735<ref>PMID:15813735</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2bgc" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_15813735}}, adds the Publication Abstract to the page
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15813735 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_15813735}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2BGC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BGC OCA].
[[Category: Listeria monocytogenes EGD-e]]
 
[[Category: Eiting M]]
==Reference==
[[Category: Hagelueken G]]
The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif., Eiting M, Hageluken G, Schubert WD, Heinz DW, Mol Microbiol. 2005 Apr;56(2):433-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15813735 15813735]
[[Category: Heinz DW]]
[[Category: Listeria monocytogenes]]
[[Category: Schubert W-D]]
[[Category: Single protein]]
[[Category: Eiting, M.]]
[[Category: Hagelueken, G.]]
[[Category: Heinz, D W.]]
[[Category: Schubert, W D.]]
[[Category: Bacterial infection,human pathogen,transcriptional regulator,transcription]]
 
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Retrieved from "https://proteopedia.org/2bgc"