View source for 4o5p


==Crystal structure of an uncharacterized protein from Pseudomonas aeruginosa==
<StructureSection load='4o5p' size='340' side='right'caption='[[4o5p]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4o5p]] 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=4O5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O5P FirstGlance]. <br>
</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></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=4o5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o5p OCA], [https://pdbe.org/4o5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o5p RCSB], [https://www.ebi.ac.uk/pdbsum/4o5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o5p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9HYV3_PSEAE Q9HYV3_PSEAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A diverse superfamily of phospholipases consisting of the type VI lipase effectors Tle1-Tle5 secreted by the bacterial type VI secretion system (T6SS) have recently been identified as antibacterial effectors that hydrolyze membrane phospholipids. These effectors show no significant homology to known lipases, and their mechanism of membrane targeting and hydrolysis of phospholipids remains unknown. Here, the crystal structure of Tle1 ( approximately 96.5 kDa) from Pseudomonas aeruginosa refined to 2.0 A resolution is reported, representing the first structure of this superfamily. Its overall structure can be divided into two distinct parts, the phospholipase catalytic module and the putative membrane-anchoring module; this arrangement has not previously been observed in known lipase structures. The phospholipase catalytic module has a canonical alpha/beta-hydrolase fold and mutation of any residue in the Ser-Asp-His catalytic triad abolishes its toxicity. The putative membrane-anchoring module adopts an open conformation composed of three amphipathic domains, and its partial folds are similar to those of several periplasmic or membrane proteins. A cell-toxicity assay revealed that the putative membrane-anchoring module is critical to Tle1 antibacterial activity. A molecular-dynamics (MD) simulation system in which the putative membrane-anchoring module embedded into a bilayer was stable over 50 ns. These structure-function studies provide insight into the hydrolysis and membrane-targeting process of the unique phospholipase Tle1.

Structure of the type VI secretion phospholipase effector Tle1 provides insight into its hydrolysis and membrane targeting.,Hu H, Zhang H, Gao Z, Wang D, Liu G, Xu J, Lan K, Dong Y Acta Crystallogr D Biol Crystallogr. 2014 Aug 1;70(Pt 8):2175-85. doi:, 10.1107/S1399004714012899. Epub 2014 Jul 25. PMID:25084336<ref>PMID:25084336</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4o5p" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Dong YH]]
[[Category: Gao ZQ]]
[[Category: Hu HD]]
[[Category: Zhang H]]