2axw: Difference between revisions

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New page: left|200px<br /><applet load="2axw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2axw, resolution 1.05Å" /> '''Structure of DraD in...
 
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[[Image:2axw.jpg|left|200px]]<br /><applet load="2axw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2axw, resolution 1.05&Aring;" />
'''Structure of DraD invasin from uropathogenic Escherichia coli'''<br />


==Overview==
==Structure of DraD invasin from uropathogenic Escherichia coli==
The dra gene cluster of uropathogenic strains of Escherichia coli produces, proteins involved in bacterial attachment to and invasion of the, eukaryotic host tissues. The crystal structure of a construct of E. coli, DraD possessing an additional C-terminal extension of 13 amino acids, including a His6 tag, has been solved at a resolution of 1.05 angstroms., The protein forms symmetric dimers through the exchange of the C-terminal, beta-strands, which participate in the immunoglobulin-like beta-sandwich, fold of each subunit. This structure confirms that DraD is able to act as, an acceptor in the donor-strand complementation mechanism of fiber, formation but, in contrast to DraE adhesin, its native sequence does not, have a donor strand; therefore, DraD can only be located at the tip of the, fiber.
<StructureSection load='2axw' size='340' side='right'caption='[[2axw]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2axw]] is a 2 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=2AXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AXW 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]] 1.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2axw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2axw OCA], [https://pdbe.org/2axw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2axw RCSB], [https://www.ebi.ac.uk/pdbsum/2axw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2axw ProSAT]</span></td></tr>
</table>
== 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/ax/2axw_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=2axw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The dra gene cluster of uropathogenic strains of Escherichia coli produces proteins involved in bacterial attachment to and invasion of the eukaryotic host tissues. The crystal structure of a construct of E. coli DraD possessing an additional C-terminal extension of 13 amino acids, including a His6 tag, has been solved at a resolution of 1.05 angstroms. The protein forms symmetric dimers through the exchange of the C-terminal beta-strands, which participate in the immunoglobulin-like beta-sandwich fold of each subunit. This structure confirms that DraD is able to act as an acceptor in the donor-strand complementation mechanism of fiber formation but, in contrast to DraE adhesin, its native sequence does not have a donor strand; therefore, DraD can only be located at the tip of the fiber.


==About this Structure==
Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails.,Jedrzejczak R, Dauter Z, Dauter M, Piatek R, Zalewska B, Mroz M, Bury K, Nowicki B, Kur J Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):157-64. Epub 2006, Jan 18. PMID:16421447<ref>PMID:16421447</ref>
2AXW 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=CL:'>CL</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXW OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails., Jedrzejczak R, Dauter Z, Dauter M, Piatek R, Zalewska B, Mroz M, Bury K, Nowicki B, Kur J, Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):157-64. Epub 2006, Jan 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16421447 16421447]
</div>
<div class="pdbe-citations 2axw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bury, K.]]
[[Category: Bury K]]
[[Category: Dauter, M.]]
[[Category: Dauter M]]
[[Category: Dauter, Z.]]
[[Category: Dauter Z]]
[[Category: Jedrzejczak, R.]]
[[Category: Jedrzejczak R]]
[[Category: Kur, J.]]
[[Category: Kur J]]
[[Category: Mroz, M.]]
[[Category: Mroz M]]
[[Category: Nowicki, B.]]
[[Category: Nowicki B]]
[[Category: Piatek, R.]]
[[Category: Piatek R]]
[[Category: Zalewska, B.]]
[[Category: Zalewska B]]
[[Category: CL]]
[[Category: GOL]]
[[Category: beta-sandwich]]
[[Category: homodimer]]
[[Category: immunoglobulin-like fold]]
[[Category: swapped c-terminal strands]]
 
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