View source for 3v16

==An intramolecular pi-cation latch in phosphatidylinositol-specific phospholipase C from S.aureus controls substrate access to the active site==
<StructureSection load='3v16' size='340' side='right' caption='[[3v16]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3v16]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus Staphylococcus aureus subsp. aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V16 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene></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=3v16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v16 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v16 RCSB], [http://www.ebi.ac.uk/pdbsum/3v16 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://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 ==
Staphylococcus aureus secretes a phosphatidylinositol-specific phospholipase C (PI-PLC) as a virulence factor that is unusual in exhibiting higher activity at acidic pH values than other enzymes in this class. We have determined the crystal structure of this enzyme at pH 4.6 and pH 7.5. Under slightly basic conditions, the S. aureus PI-PLC structure closely follows the conformation of other bacterial PI-PLCs. However, when crystallized under acidic conditions, a large section of mobile loop at the alphabeta-barrel rim in the vicinity of the active site shows approximately 10 A shift. This loop displacement at acidic pH is the result of a titratable intramolecular pi-cation interaction between His258 and Phe249. This was verified by a structure of the mutant protein H258Y crystallized at pH 4.6, which does not exhibit the large loop shift. The intramolecular pi-cation interaction for S. aureus PI-PLC provides an explanation for the activity of the enzyme at acid pH and also suggests how phosphatidylcholine, as a competitor for Phe249, may kinetically activate this enzyme.

Structure of the S. aureus PI-Specific Phospholipase C Reveals Modulation of Active Site Access by a Titratable pi-Cation Latched Loop.,Goldstein R, Cheng J, Stec B, Roberts MF Biochemistry. 2012 Mar 27;51(12):2579-87. Epub 2012 Mar 16. PMID:22390775<ref>PMID:22390775</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>

==See Also==
*[[Phosphatidylinositol-specific phospholipase C|Phosphatidylinositol-specific phospholipase C]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Phosphatidylinositol diacylglycerol-lyase]]
[[Category: Staphylococcus aureus subsp. aureus]]
[[Category: Cheng, J]]
[[Category: Goldstein, R I]]
[[Category: Roberts, M F]]
[[Category: Stec, B]]
[[Category: Lyase]]
[[Category: Phospholipase]]
[[Category: Pi-cation]]
[[Category: Tim barrel]]