4aur: Difference between revisions

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New page: '''Unreleased structure''' The entry 4aur is ON HOLD until Paper Publication Authors: Michie, K.A., Low, H.H., Lowe, J. Description: LeoA bacterial dynamin GTPase from ETEC
 
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'''Unreleased structure'''


The entry 4aur is ON HOLD  until Paper Publication
==LeoA bacterial dynamin GTPase from ETEC==
<StructureSection load='4aur' size='340' side='right'caption='[[4aur]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4aur]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_ETEC_H10407 Escherichia coli ETEC H10407]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AUR 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4aur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aur OCA], [https://pdbe.org/4aur PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aur RCSB], [https://www.ebi.ac.uk/pdbsum/4aur PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aur ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Escherichia coli (ETEC) strain H10407 contains a GTPase virulence factor, LeoA, which is encoded on a pathogenicity island and has been shown to enhance toxin release, potentially through vesicle secretion. By sequence comparisons and X-ray structure determination we now identify LeoA as a bacterial dynamin-like protein (DLP). Proteins of the dynamin family remodel membranes and were once thought to be restricted to eukaryotes. In ETEC H10407 LeoA localises to the periplasm where it forms a punctate localisation pattern. Bioinformatic analyses of leoA and the two upstream genes leoB and leoC suggest that LeoA works in concert with a second dynamin-like protein, made up of LeoB and LeoC. Disruption of the leoAB genes leads to a reduction in secretion of periplasmic Tat-GFP and outer membrane OmpA. Our data suggest a role for LeoABC dynamin-like proteins in potentiating virulence through membrane vesicle associated toxin secretion.


Authors: Michie, K.A., Low, H.H., Lowe, J.
LeoA, B and C from Enterotoxigenic Escherichia coli (ETEC) Are Bacterial Dynamins.,Michie KA, Boysen A, Low HH, Moller-Jensen J, Lowe J PLoS One. 2014 Sep 9;9(9):e107211. doi: 10.1371/journal.pone.0107211. eCollection, 2014. PMID:25203511<ref>PMID:25203511</ref>


Description: LeoA bacterial dynamin GTPase from ETEC
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4aur" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli ETEC H10407]]
[[Category: Large Structures]]
[[Category: Low HH]]
[[Category: Lowe J]]
[[Category: Michie KA]]

Latest revision as of 02:41, 21 November 2024

LeoA bacterial dynamin GTPase from ETEC

4aur, resolution 2.70Å

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