2w7q
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2w7q is ON HOLD until Paper Publication Authors: Remans, K., Pauwels, K., van Ulsen, P., Savvides, S., Decanniere, K., Cornelis, P., Tommassen, J., ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Pseudomonas aeruginosa LolA== | |
| + | <StructureSection load='2w7q' size='340' side='right'caption='[[2w7q]], [[Resolution|resolution]] 1.88Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2w7q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W7Q 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]] 1.88Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2w7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w7q OCA], [https://pdbe.org/2w7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w7q RCSB], [https://www.ebi.ac.uk/pdbsum/2w7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w7q ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LOLA_PSEAE LOLA_PSEAE] Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).[HAMAP-Rule:MF_00240] | ||
| + | == 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/w7/2w7q_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=2w7q ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Many lipoproteins reside in the outer membrane (OM) of Gram-negative bacteria, and their biogenesis is dependent on the Lol (localization of lipoproteins) system. The periplasmic chaperone LolA accepts OM-destined lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. The exact nature of the LolA-lipoprotein complex is still unknown. The crystal structure of Escherichia coli LolA features an open beta-barrel covered by alpha helices that together constitute a hydrophobic cavity, which would allow the binding of one acyl chain. However, OM lipoproteins contain three acyl chains, and the stoichiometry of the LolA-lipoprotein complex is 1:1. Here we present the crystal structure of Pseudomonas aeruginosa LolA that projects clear hydrophobic surface patches. Since these patches are large enough to accommodate acyl chains, their role in lipoprotein binding was investigated. Several LolA mutant proteins were created, and their functionality was assessed by studying their capacity to release lipoproteins produced in sphaeroplasts. Interruption of the largest hydrophobic patch completely destroyed the lipoprotein-releasing capacity of LolA, while interruption of smaller patches apparently reduced efficiency. Thus, the results show a new lipoprotein transport model that places (some of) the acyl chains on the hydrophobic surface patches. | ||
| - | + | Hydrophobic surface patches on LolA of Pseudomonas aeruginosa are essential for lipoprotein binding.,Remans K, Pauwels K, van Ulsen P, Buts L, Cornelis P, Tommassen J, Savvides SN, Decanniere K, Van Gelder P J Mol Biol. 2010 Sep 3;401(5):921-30. Epub 2010 Jul 8. PMID:20620146<ref>PMID:20620146</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2w7q" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas aeruginosa PAO1]] | ||
| + | [[Category: Cornelis P]] | ||
| + | [[Category: Decanniere K]] | ||
| + | [[Category: Pauwels K]] | ||
| + | [[Category: Remans K]] | ||
| + | [[Category: Savvides S]] | ||
| + | [[Category: Tommassen J]] | ||
| + | [[Category: Van Gelder P]] | ||
| + | [[Category: Van Ulsen P]] | ||
Current revision
Structure of Pseudomonas aeruginosa LolA
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