View source for 5ovm


==Solution structure of lipase binding domain LID1 of foldase from Pseudomonas aeruginosa==
<StructureSection load='5ovm' size='340' side='right'caption='[[5ovm]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ovm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OVM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5ovm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ovm OCA], [https://pdbe.org/5ovm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ovm RCSB], [https://www.ebi.ac.uk/pdbsum/5ovm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ovm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LIFO_PSEAE LIFO_PSEAE] May be involved in the folding of the extracellular lipase during its passage through the periplasm.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Folding and cellular localization of many proteins of Gram-negative bacteria rely on a network of chaperones and secretion systems. Among them is the lipase-specific foldase Lif, a membrane-bound steric chaperone that tightly binds (KD = 29 nM) and mediates folding of the lipase LipA, a virulence factor of the pathogenic bacterium P. aeruginosa. Lif consists of five-domains, including a mini domain MD1 essential for LipA folding. However, the molecular mechanism of Lif-assisted LipA folding remains elusive. Here, we show in in vitro experiments using a soluble form of Lif (sLif) that isolated MD1 inhibits sLif-assisted LipA activation. Furthermore, the ability to activate LipA is lost in the variant sLifY99A, in which the evolutionary conserved amino acid Y99 from helix alpha1 of MD1 is mutated to alanine. This coincides with an approximately three-fold reduced affinity of the variant to LipA together with increased flexibility of sLifY99A in the complex as determined by polarization-resolved fluorescence spectroscopy. We have solved the NMR solution structures of P. aeruginosa MD1 and variant MD1Y99A revealing a similar fold indicating that a structural modification is likely not the reason for the impaired activity of variant sLifY99A. Molecular dynamics simulations of the sLif:LipA complex in connection with rigidity analyses suggest a long-range network of interactions spanning from Y99 of sLif to the active site of LipA, which might be essential for LipA activation. These findings provide important details about the putative mechanism for LipA activation and point to a general mechanism of protein folding by multi-domain steric chaperones.

Structural and dynamic insights revealing how lipase binding domain MD1 of Pseudomonas aeruginosa foldase affects lipase activation.,Viegas A, Dollinger P, Verma N, Kubiak J, Viennet T, Seidel CAM, Gohlke H, Etzkorn M, Kovacic F, Jaeger KE Sci Rep. 2020 Feb 27;10(1):3578. doi: 10.1038/s41598-020-60093-4. PMID:32107397<ref>PMID:32107397</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ovm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Dollinger P]]
[[Category: Etzkorn M]]
[[Category: Gohlke H]]
[[Category: Jaeger K-E]]
[[Category: Kovacic F]]
[[Category: Verma N]]
[[Category: Viegas A]]