View source for 6hsy


==Two-phospholipid-bound crystal structure of the substrate-binding protein Ttg2D from Pseudomonas aeruginosa==
<StructureSection load='6hsy' size='340' side='right'caption='[[6hsy]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hsy]] is a 1 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=6HSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HSY 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]] 2.53&#8491;</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>, <scene name='pdbligand=GOT:Phospholipid+PG(16 0/cy17 0)'>GOT</scene>, <scene name='pdbligand=H3T:Phospholipid+PG(16 0/cy17 0)'>H3T</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=6hsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hsy OCA], [https://pdbe.org/6hsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hsy RCSB], [https://www.ebi.ac.uk/pdbsum/6hsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hsy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9HVW4_PSEAE Q9HVW4_PSEAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In Pseudomonas aeruginosa, Ttg2D is the soluble periplasmic phospholipid-binding component of an ABC transport system thought to be involved in maintaining the asymmetry of the outer membrane. Here we use the crystallographic structure of Ttg2D at 2.5 A resolution to reveal that this protein can accommodate four acyl chains. Analysis of the available structures of Ttg2D orthologs shows that they conform a new substrate-binding-protein structural cluster. Native and denaturing mass spectrometry experiments confirm that Ttg2D, produced both heterologously and homologously and isolated from the periplasm, can carry two diacyl glycerophospholipids as well as one cardiolipin. Binding is notably promiscuous, allowing the transport of various molecular species. In vitro binding assays coupled to native mass spectrometry show that binding of cardiolipin is spontaneous. Gene knockout experiments in P. aeruginosa multidrug-resistant strains reveal that the Ttg2 system is involved in low-level intrinsic resistance against certain antibiotics that use a lipid-mediated pathway to permeate through membranes.

The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm.,Yero D, Diaz-Lobo M, Costenaro L, Conchillo-Sole O, Mayo A, Ferrer-Navarro M, Vilaseca M, Gibert I, Daura X Commun Biol. 2021 Apr 9;4(1):448. doi: 10.1038/s42003-021-01968-8. PMID:33837253<ref>PMID:33837253</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6hsy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Conchillo-Sole O]]
[[Category: Costenaro L]]
[[Category: Daura X]]