2axw: Difference between revisions
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< | ==Structure of DraD invasin from uropathogenic Escherichia coli== | ||
<StructureSection load='2axw' size='340' side='right'caption='[[2axw]], [[Resolution|resolution]] 1.05Å' 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]] 1.05Å</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. | 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. | ||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2axw" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bury | [[Category: Bury K]] | ||
[[Category: Dauter | [[Category: Dauter M]] | ||
[[Category: Dauter | [[Category: Dauter Z]] | ||
[[Category: Jedrzejczak | [[Category: Jedrzejczak R]] | ||
[[Category: Kur | [[Category: Kur J]] | ||
[[Category: Mroz | [[Category: Mroz M]] | ||
[[Category: Nowicki | [[Category: Nowicki B]] | ||
[[Category: Piatek | [[Category: Piatek R]] | ||
[[Category: Zalewska | [[Category: Zalewska B]] | ||
