5fqu: Difference between revisions
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==Orthorhombic crystal structure of of PlpD (selenomethionine derivative)== | |||
<StructureSection load='5fqu' size='340' side='right' caption='[[5fqu]], [[Resolution|resolution]] 2.74Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fqu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FQU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FQU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fqu OCA], [http://pdbe.org/5fqu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fqu RCSB], [http://www.ebi.ac.uk/pdbsum/5fqu PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The type V secretion system is a macromolecular machine employed by a number of bacteria to secrete virulence factors into the environment. The human pathogen Pseudomonas aeruginosa employs the newly described type Vd secretion system to secrete a soluble variant of PlpD, a lipase of the patatin-like family synthesized as a single macromolecule that also carries a polypeptide transport-associated domain and a 16-stranded beta-barrel. Here we report the crystal structure of the secreted form of PlpD in its biologically active state. PlpD displays a classical lipase alpha/beta hydrolase fold with a catalytic site located within a highly hydrophobic channel that entraps a lipidic molecule. The active site is covered by a flexible lid, as in other lipases, indicating that this region in PlpD must modify its conformation in order for catalysis at the water-lipid interface to occur. PlpD displays phospholipase A1 activity and is able to recognize a number of phosphatidylinositols and other phosphatidyl analogs. PlpD is the first example of an active phospholipase secreted through the type V secretion system, for which there are more than 200 homologs, revealing details of the lipid destruction arsenal expressed by P. aeruginosa in order to establish infection. | |||
Structural Basis of Lipid Targeting and Destruction by the Type V Secretion System of Pseudomonas aeruginosa.,da Mata Madeira PV, Zouhir S, Basso P, Neves D, Laubier A, Salacha R, Bleves S, Faudry E, Contreras-Martel C, Dessen A J Mol Biol. 2016 May 8;428(9 Pt A):1790-803. doi: 10.1016/j.jmb.2016.03.012. Epub, 2016 Mar 21. PMID:27012424<ref>PMID:27012424</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5fqu" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Basso, P]] | |||
[[Category: Bleves, S]] | |||
[[Category: Contreras-Martel, C]] | |||
[[Category: Dessen, A]] | [[Category: Dessen, A]] | ||
[[Category: Faudry, E]] | |||
[[Category: Laubier, A]] | |||
[[Category: Madeira, P Vinicius da Mata]] | |||
[[Category: Neves, D]] | [[Category: Neves, D]] | ||
[[Category: Salacha, R]] | [[Category: Salacha, R]] | ||
[[Category: Zouhir, S]] | [[Category: Zouhir, S]] | ||
[[Category: | [[Category: Bacterial secretion]] | ||
[[Category: | [[Category: Infection]] | ||
[[Category: | [[Category: Lipid affinity]] | ||
[[Category: Phospholipase]] | |||
[[Category: Transport protein]] | |||