View source for 9bsm


==Staphylococcus aureus exfoliative toxin A D164E variant==
<StructureSection load='9bsm' size='340' side='right'caption='[[9bsm]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9bsm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BSM 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]] 1.48&#8491;</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=9bsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bsm OCA], [https://pdbe.org/9bsm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bsm RCSB], [https://www.ebi.ac.uk/pdbsum/9bsm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bsm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ETA_STAAU ETA_STAAU] Has serine protease-like properties and binds to the skin protein profilaggrin. Cleaves substrates after acidic residues. Exfoliative toxins cause impetigous diseases commonly referred as staphylococcal scalded skin syndrome (SSSS).<ref>PMID:2117445</ref> <ref>PMID:2384148</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Serine proteases have been proposed to dynamically sample inactive and active conformations, but direct evidence at atomic resolution has remained elusive. Using nuclear magnetic resonance (NMR), we identified a single residue, D164, in exfoliative toxin A (ETA) that acts as a molecular "switch" to regulate global dynamic sampling. Mutations at this site shift the balance between inactive and active states, correlating directly with catalytic activity. Beyond identifying this dynamic switch, we demonstrate how it works in concert with other allosterically coupled sites to rationally control enzyme movements and catalytic function. This study provides a framework for linking conformational dynamics to function and paves the way for engineering enzymes, in particular, proteases, with tailored activities for applications in medicine and biotechnology.

Identifying and controlling inactive and active conformations of a serine protease.,Lee E, Tran N, Redzic JS, Singh H, Alamillo L, Holyoak T, Hamelberg D, Eisenmesser EZ Sci Adv. 2025 Apr 11;11(15):eadu7447. doi: 10.1126/sciadv.adu7447. Epub 2025 Apr , 9. PMID:40203097<ref>PMID:40203097</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9bsm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Holyoak T]]
[[Category: Tran N]]