View source for 4i90


==Structure of the N254Y/H258Y mutant of the phosphatidylinositol-specific phospholipase C from S. aureus bound to choline==
<StructureSection load='4i90' size='340' side='right'caption='[[4i90]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4i90]] 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=4I90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I90 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]] 1.65&#8491;</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=CHT:CHOLINE+ION'>CHT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4i90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i90 OCA], [https://pdbe.org/4i90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i90 RCSB], [https://www.ebi.ac.uk/pdbsum/4i90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i90 ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== 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<ref>PMID:23576432</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4i90" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phospholipase C|Phospholipase C]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus str. Newman]]
[[Category: Cheng J]]
[[Category: Gershenson A]]
[[Category: Goldstein RI]]
[[Category: Roberts MF]]
[[Category: Stec B]]