2j6g: Difference between revisions

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[[Image:2j6g.gif|left|200px]]<br /><applet load="2j6g" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2j6g, resolution 1.55&Aring;" />
'''FAEG FROM F4AC ETEC STRAIN 5_95, PRODUCED IN TOBACCO PLANT CHLOROPLAST'''<br />


==Overview==
==FaeG from F4ac ETEC strain 5_95, produced in tobacco plant chloroplast==
<StructureSection load='2j6g' size='340' side='right'caption='[[2j6g]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2j6g]] 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=2J6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J6G FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j6g OCA], [https://pdbe.org/2j6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j6g RCSB], [https://www.ebi.ac.uk/pdbsum/2j6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j6g ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6T3W5_ECOLX Q6T3W5_ECOLX]
== 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/j6/2j6g_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=2j6g ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
F4 fimbriae encoded by the fae operon are the major colonization factors associated with porcine neonatal and postweaning diarrhoea caused by enterotoxigenic Escherichia coli (ETEC). Via the chaperone/usher pathway, the F4 fimbriae are assembled as long polymers of the major subunit FaeG, which also possesses the adhesive properties of the fimbriae. Intrinsically, the incomplete fold of fimbrial subunits renders them unstable and susceptible to aggregation and/or proteolytic degradation in the absence of a specific periplasmic chaperone. In order to test the possibility of producing FaeG in plants, FaeG expression was studied in transgenic tobacco plants. FaeG was directed to different subcellular compartments by specific targeting signals. Targeting of FaeG to the chloroplast results in much higher yields than FaeG targeting to the endoplasmic reticulum or the apoplast. Two chloroplast-targeted FaeG variants were purified from tobacco plants and crystallized. The crystal structures show that chloroplasts circumvent the absence of the fimbrial assembly machinery by assembling FaeG into strand-swapped dimers. Furthermore, the structures reveal how FaeG combines the structural requirements of a major fimbrial subunit with its adhesive role by grafting an additional domain on its Ig-like core.
F4 fimbriae encoded by the fae operon are the major colonization factors associated with porcine neonatal and postweaning diarrhoea caused by enterotoxigenic Escherichia coli (ETEC). Via the chaperone/usher pathway, the F4 fimbriae are assembled as long polymers of the major subunit FaeG, which also possesses the adhesive properties of the fimbriae. Intrinsically, the incomplete fold of fimbrial subunits renders them unstable and susceptible to aggregation and/or proteolytic degradation in the absence of a specific periplasmic chaperone. In order to test the possibility of producing FaeG in plants, FaeG expression was studied in transgenic tobacco plants. FaeG was directed to different subcellular compartments by specific targeting signals. Targeting of FaeG to the chloroplast results in much higher yields than FaeG targeting to the endoplasmic reticulum or the apoplast. Two chloroplast-targeted FaeG variants were purified from tobacco plants and crystallized. The crystal structures show that chloroplasts circumvent the absence of the fimbrial assembly machinery by assembling FaeG into strand-swapped dimers. Furthermore, the structures reveal how FaeG combines the structural requirements of a major fimbrial subunit with its adhesive role by grafting an additional domain on its Ig-like core.


==About this Structure==
Chloroplasts assemble the major subunit FaeG of Escherichia coli F4 (K88) fimbriae to strand-swapped dimers.,Van Molle I, Joensuu JJ, Buts L, Panjikar S, Kotiaho M, Bouckaert J, Wyns L, Niklander-Teeri V, De Greve H J Mol Biol. 2007 May 4;368(3):791-9. Epub 2007 Feb 22. PMID:17368480<ref>PMID:17368480</ref>
2J6G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J6G OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Chloroplasts assemble the major subunit FaeG of Escherichia coli F4 (K88) fimbriae to strand-swapped dimers., Van Molle I, Joensuu JJ, Buts L, Panjikar S, Kotiaho M, Bouckaert J, Wyns L, Niklander-Teeri V, De Greve H, J Mol Biol. 2007 May 4;368(3):791-9. Epub 2007 Feb 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17368480 17368480]
</div>
<div class="pdbe-citations 2j6g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bouckaert, J.]]
[[Category: Bouckaert J]]
[[Category: Buts, L.]]
[[Category: Buts L]]
[[Category: Greve, H De.]]
[[Category: De Greve H]]
[[Category: Joensuu, J J.]]
[[Category: Joensuu JJ]]
[[Category: Kotiaho, M.]]
[[Category: Kotiaho M]]
[[Category: Molle, I Van.]]
[[Category: Niklander-Teeri V]]
[[Category: Niklander-Teeri, V.]]
[[Category: Panjikar S]]
[[Category: Panjikar, S.]]
[[Category: Van Molle I]]
[[Category: Wyns, L.]]
[[Category: Wyns L]]
[[Category: ACT]]
[[Category: cell adhesion]]
[[Category: chaperone-usher pathway]]
[[Category: chloroplast targeting]]
[[Category: f4 fimbriae]]
[[Category: ig-fold]]
[[Category: strand swapping]]
 
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