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| | ==Structure of the N254Y/H258Y double mutant of the Phosphatidylinositol-Specific Phospholipase C from S.aureus== | | ==Structure of the N254Y/H258Y double mutant of the Phosphatidylinositol-Specific Phospholipase C from S.aureus== |
| - | <StructureSection load='4f2u' size='340' side='right' caption='[[4f2u]], [[Resolution|resolution]] 2.19Å' scene=''> | + | <StructureSection load='4f2u' size='340' side='right'caption='[[4f2u]], [[Resolution|resolution]] 2.19Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4f2u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staae Staae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F2U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F2U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4f2u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_str._Newman Staphylococcus aureus subsp. aureus str. Newman]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F2U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v16|3v16]], [[3v18|3v18]], [[3v1h|3v1h]], [[4f2b|4f2b]], [[4f2t|4f2t]]</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=4f2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f2u OCA], [https://pdbe.org/4f2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f2u RCSB], [https://www.ebi.ac.uk/pdbsum/4f2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f2u ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">plc, NWMN_0041 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=426430 STAAE])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] </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=4f2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f2u OCA], [http://pdbe.org/4f2u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f2u RCSB], [http://www.ebi.ac.uk/pdbsum/4f2u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f2u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PLC_STAAE PLC_STAAE]] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor. | + | [https://www.uniprot.org/uniprot/PLC_STAAE PLC_STAAE] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Phosphatidylinositol diacylglycerol-lyase]] | + | [[Category: Large Structures]] |
| - | [[Category: Staae]] | + | [[Category: Staphylococcus aureus subsp. aureus str. Newman]] |
| - | [[Category: Cheng, J]] | + | [[Category: Cheng J]] |
| - | [[Category: Gershenson, A]] | + | [[Category: Gershenson A]] |
| - | [[Category: Goldstein, R]] | + | [[Category: Goldstein R]] |
| - | [[Category: Roberts, M F]] | + | [[Category: Roberts MF]] |
| - | [[Category: Stec, B]] | + | [[Category: Stec B]] |
| - | [[Category: Alpha beta barrel]]
| + | |
| - | [[Category: Lyase]]
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| - | [[Category: Membrane interface]]
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| - | [[Category: Phosphatidylinositol-specific phospholipase c]]
| + | |
| Structural highlights
Function
PLC_STAAE Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor.
Publication Abstract from PubMed
Staphylococcus aureus phosphatidylinositol-specific phospholipase C (PI-PLC) is a secreted virulence factor for this pathogenic bacterium. A novel crystal structure shows that this PI-PLC can form a dimer via helix B, a structural feature present in all secreted, bacterial PI-PLCs that is important for membrane binding. Despite the small size of this interface, it is critical for optimal enzyme activity. Kinetic evidence, increased enzyme specific activity with increasing enzyme concentration, supports a mechanism where the PI-PLC dimerization is enhanced in membranes containing phosphatidylcholine (PC). Mutagenesis of key residues confirm that the zwitterionic phospholipid acts not by specific binding to the protein, but rather by reducing anionic lipid interactions with a cationic pocket on the surface of the S. aureus enzyme that stabilizes monomeric protein. Despite its structural and sequence similarity to PI-PLCs from other Gram-positive pathogenic bacteria, S. aureus PI-PLC appears to have a unique mechanism where enzyme activity is modulated by competition between binding of soluble anions or anionic lipids to the cationic sensor and transient dimerization on the membrane.
Competition between Anion Binding and Dimerization Modulates Staphylococcus aureus Phosphatidylinositol-specific Phospholipase C Enzymatic Activity.,Cheng J, Goldstein R, Stec B, Gershenson A, Roberts MF J Biol Chem. 2012 Nov 23;287(48):40317-27. doi: 10.1074/jbc.M112.395277. Epub, 2012 Oct 4. PMID:23038258[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cheng J, Goldstein R, Stec B, Gershenson A, Roberts MF. Competition between Anion Binding and Dimerization Modulates Staphylococcus aureus Phosphatidylinositol-specific Phospholipase C Enzymatic Activity. J Biol Chem. 2012 Nov 23;287(48):40317-27. doi: 10.1074/jbc.M112.395277. Epub, 2012 Oct 4. PMID:23038258 doi:http://dx.doi.org/10.1074/jbc.M112.395277
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