4f2t: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4f2t]] 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=4F2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F2T FirstGlance]. <br>
<table><tr><td colspan='2'>[[4f2t]] 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=4F2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F2T 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></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]] 2.3&#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></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=4f2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f2t OCA], [https://pdbe.org/4f2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f2t RCSB], [https://www.ebi.ac.uk/pdbsum/4f2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f2t ProSAT]</span></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=4f2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f2t OCA], [https://pdbe.org/4f2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f2t RCSB], [https://www.ebi.ac.uk/pdbsum/4f2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f2t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://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;">
== 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<ref>PMID:23038258</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4f2t" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Phospholipase C|Phospholipase C]]
*[[Phospholipase C|Phospholipase C]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 18:14, 14 March 2024

Modulation of S.aureus Phosphatidylinositol-Specific Phospholipase C Membrane Binding.Modulation of S.aureus Phosphatidylinositol-Specific Phospholipase C Membrane Binding.

Structural highlights

4f2t is a 1 chain structure with sequence from Staphylococcus aureus subsp. aureus str. Newman. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PLC_STAAE Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor.

See Also

4f2t, resolution 2.30Å

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