9BSH
Staphylococcus aureus exfoliative toxin A D164A variant
Summary for 9BSH
| Entry DOI | 10.2210/pdb9bsh/pdb |
| Descriptor | Exfoliative toxin A (2 entities in total) |
| Functional Keywords | exfoliative toxin, toxin |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 2 |
| Total formula weight | 62182.12 |
| Authors | |
| Primary citation | Lee, E.,Tran, N.,Redzic, J.S.,Singh, H.,Alamillo, L.,Holyoak, T.,Hamelberg, D.,Eisenmesser, E.Z. Identifying and controlling inactive and active conformations of a serine protease. Sci Adv, 11:eadu7447-eadu7447, 2025 Cited by PubMed Abstract: 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. PubMed: 40203097DOI: 10.1126/sciadv.adu7447 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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