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| | <StructureSection load='5dir' size='340' side='right'caption='[[5dir]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='5dir' size='340' side='right'caption='[[5dir]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dir]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DIR FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lspA, ls, PA4559 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Signal_peptidase_II Signal peptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.36 3.4.23.36] </span></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=5dir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dir OCA], [http://pdbe.org/5dir PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dir RCSB], [http://www.ebi.ac.uk/pdbsum/5dir PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dir ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LSPA_PSEAE LSPA_PSEAE]] This protein specifically catalyzes the removal of signal peptides from prolipoproteins. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Signal peptidase II]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Arnaout, T El]]
| + | [[Category: Bailey J]] |
| - | [[Category: Bailey, J]] | + | [[Category: Boland C]] |
| - | [[Category: Boland, C]] | + | [[Category: Caffrey M]] |
| - | [[Category: Caffrey, M]] | + | [[Category: El Arnaout T]] |
| - | [[Category: Vogeley, L]] | + | [[Category: Vogeley L]] |
| - | [[Category: Antibiotic]] | + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Protease]]
| + | |
| Structural highlights
5dir is a 8 chain structure with sequence from Pseudomonas aeruginosa PAO1 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.8Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
LSPA_PSEAE This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vogeley L, El Arnaout T, Bailey J, Stansfeld PJ, Boland C, Caffrey M. Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin. Science. 2016 Feb 19;351(6275):876-80. doi: 10.1126/science.aad3747. PMID:26912896 doi:http://dx.doi.org/10.1126/science.aad3747
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