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| | ==Structure of the unliganded N254Y/H258Y mutant of the phosphatidylinositol-specific phospholipase C from S. aureus== | | ==Structure of the unliganded N254Y/H258Y mutant of the phosphatidylinositol-specific phospholipase C from S. aureus== |
| - | <StructureSection load='4i8y' size='340' side='right' caption='[[4i8y]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='4i8y' size='340' side='right'caption='[[4i8y]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i8y]] 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=4I8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I8Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4i8y]] 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=4I8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I8Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i90|4i90]], [[4i9m|4i9m]], [[4i9t|4i9t]]</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=4i8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i8y OCA], [https://pdbe.org/4i8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i8y RCSB], [https://www.ebi.ac.uk/pdbsum/4i8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i8y 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=4i8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i8y OCA], [http://pdbe.org/4i8y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i8y RCSB], [http://www.ebi.ac.uk/pdbsum/4i8y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i8y 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 I]] | + | [[Category: Goldstein RI]] |
| - | [[Category: Roberts, M F]] | + | [[Category: Roberts MF]] |
| - | [[Category: Stec, B]] | + | [[Category: Stec B]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lyase]]
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| - | [[Category: Phospholipase]]
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| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
PLC_STAAE Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor.
Publication Abstract from PubMed
Peripheral membrane proteins can be targeted to specific organelles or the plasma membrane by differential recognition of phospholipid headgroups. Although molecular determinants of specificity for several headgroups, including phosphatidylserine and phosphoinositides are well defined, specific recognition of the headgroup of the zwitterionic phosphatidylcholine (PC) is less well understood. In cytosolic proteins the cation-pi box provides a suitable receptor for choline recognition and binding through the trimethylammonium moiety. In PC, this moiety might provide a sufficient handle to bind to peripheral proteins via a cation-pi cage, where the pi systems of two or more aromatic residues are within 4-5 A of the quaternary amine. We prove this hypothesis by engineering the cation-pi box into secreted phosphatidylinositol-specific phospholipase C from Staphylococcus aureus, which lacks specific PC recognition. The N254Y/H258Y variant selectively binds PC-enriched vesicles, and x-ray crystallography reveals N254Y/H258Y binds choline and dibutyroylphosphatidylcholine within the cation-pi motif. Such simple PC recognition motifs could be engineered into a wide variety of secondary structures providing a generally applicable method for specific recognition of PC.
The cation-pi box is a specific phosphatidylcholine membrane targeting motif.,Cheng J, Goldstein R, Gershenson A, Stec B, Roberts MF J Biol Chem. 2013 May 24;288(21):14863-73. doi: 10.1074/jbc.M113.466532. Epub, 2013 Apr 10. PMID:23576432[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cheng J, Goldstein R, Gershenson A, Stec B, Roberts MF. The cation-pi box is a specific phosphatidylcholine membrane targeting motif. J Biol Chem. 2013 May 24;288(21):14863-73. doi: 10.1074/jbc.M113.466532. Epub, 2013 Apr 10. PMID:23576432 doi:http://dx.doi.org/10.1074/jbc.M113.466532
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