View source for 5dir


==membrane protein at 2.8 Angstroms==
<StructureSection load='5dir' size='340' side='right'caption='[[5dir]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dir]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DIR 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5BV:(2R,3R)-3-(GLYCYLOXY)-2-METHYLNONANOIC+ACID'>5BV</scene>, <scene name='pdbligand=ALO:ALLO-THREONINE'>ALO</scene>, <scene name='pdbligand=IIL:ISO-ISOLEUCINE'>IIL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PRD_002257:Globomycin'>PRD_002257</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=5dir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dir OCA], [https://pdbe.org/5dir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dir RCSB], [https://www.ebi.ac.uk/pdbsum/5dir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dir ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LSPA_PSEAE LSPA_PSEAE] This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
With functions that range from cell envelope structure to signal transduction and transport, lipoproteins constitute 2 to 3% of bacterial genomes and play critical roles in bacterial physiology, pathogenicity, and antibiotic resistance. Lipoproteins are synthesized with a signal peptide securing them to the cytoplasmic membrane with the lipoprotein domain in the periplasm or outside the cell. Posttranslational processing requires a signal peptidase II (LspA) that removes the signal peptide. Here, we report the crystal structure of LspA from Pseudomonas aeruginosa complexed with the antimicrobial globomycin at 2.8 angstrom resolution. Mutagenesis studies identify LspA as an aspartyl peptidase. In an example of molecular mimicry, globomycin appears to inhibit by acting as a noncleavable peptide that sterically blocks the active site. This structure should inform rational antibiotic drug discovery.

Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin.,Vogeley L, El Arnaout T, Bailey J, Stansfeld PJ, Boland C, Caffrey M Science. 2016 Feb 19;351(6275):876-80. doi: 10.1126/science.aad3747. PMID:26912896<ref>PMID:26912896</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dir" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Synthetic construct]]
[[Category: Bailey J]]
[[Category: Boland C]]
[[Category: Caffrey M]]
[[Category: El Arnaout T]]
[[Category: Vogeley L]]