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| | <StructureSection load='4rv3' size='340' side='right'caption='[[4rv3]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4rv3' size='340' side='right'caption='[[4rv3]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rv3]] 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=4RV3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4RV3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rv3]] 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=4RV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RV3 FirstGlance]. <br> |
| - | </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=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</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]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PF5:2,3,4,5,6-PENTAFLUORO-L-PHENYLALANINE'>PF5</scene></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=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene>, <scene name='pdbligand=PF5:2,3,4,5,6-PENTAFLUORO-L-PHENYLALANINE'>PF5</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v16|3v16]]</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=4rv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv3 OCA], [https://pdbe.org/4rv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rv3 RCSB], [https://www.ebi.ac.uk/pdbsum/4rv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rv3 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/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>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4rv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv3 OCA], [http://pdbe.org/4rv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rv3 RCSB], [http://www.ebi.ac.uk/pdbsum/4rv3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rv3 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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphatidylinositol diacylglycerol-lyase]] | + | [[Category: Staphylococcus aureus subsp. aureus str. Newman]] |
| - | [[Category: Staae]]
| + | [[Category: Eyles SJ]] |
| - | [[Category: Eyles, S J]] | + | [[Category: Gao J]] |
| - | [[Category: Gao, J]] | + | [[Category: Gershenson A]] |
| - | [[Category: Gershenson, A]] | + | [[Category: He T]] |
| - | [[Category: He, T]] | + | [[Category: Roberts MF]] |
| - | [[Category: Roberts, M F]] | + | |
| - | [[Category: Cation-pi]]
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| - | [[Category: Encoded unnatural amino acid phospholipase]]
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| - | [[Category: Lyase]]
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| - | [[Category: Tim barrel]]
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| Structural highlights
Function
PLC_STAAE Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor.
Publication Abstract from PubMed
Cation-pi interactions, where protein aromatic residues supply pi systems while positive charged portion of phospholipid head groups are the cations, have been suggested as important binding modes for peripheral membrane proteins. However, aromatic amino acids can also insert into membranes and hydrophobically interact with lipid tails. Heretofore there has been no facile way to differentiate these two types of interactions. We show that specific incorporation of fluorinated amino acids into proteins can experimentally distinguish cation-pi interactions from membrane insertion of the aromatic side-chains. Fluorinated aromatic amino acids destabilize the cation-pi interactions by altering electrostatics of the aromatic ring while their increased hydrophobicity enhances membrane insertion. Incorporation of pentafluorophenylalanine or difluorotyrosine into a Staphylococcus aureus phosphatidylinositol-specific phospholipase C (PI-PLC) variant engineered to contain a specific PC-binding site demonstrates the effectiveness of this methodology. Applying this methodology to the plethora of tyrosine residues in Bacillus thuringiensis PI-PLC definitively identifies those involved in cation-pi interactions with PC. This powerful method can easily be used to determine the roles of aromatic residues in other peripheral membrane proteins and in integral membrane proteins.
Fluorinated aromatic amino acids distinguish cation-pi interactions from membrane insertion.,He T, Gershenson A, Eyles SJ, Lee YJ, Liu WR, Wang J, Gao J, Roberts MF J Biol Chem. 2015 Jun 19. pii: jbc.M115.668343. PMID:26092728[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ He T, Gershenson A, Eyles SJ, Lee YJ, Liu WR, Wang J, Gao J, Roberts MF. Fluorinated aromatic amino acids distinguish cation-pi interactions from membrane insertion. J Biol Chem. 2015 Jun 19. pii: jbc.M115.668343. PMID:26092728 doi:http://dx.doi.org/10.1074/jbc.M115.668343
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