Our new PNAS paper just out

Our PNAS article, “Unique structural and ligand binding properties of the Staphylococcus aureus serine hydrolase FphE”, has published and is now available at: www.pnas.org/doi/10.1073/pnas.2532683123 with DOI number 10.1073/pnas.2532683123.

Between 2022 and 2024 we crystallised and examined hundreds of protein crystals of the protein FphE from Staphylococcus aureus. Now the results are finally published, revealing a highly unique dimer arrangement of FphE. This arrangement has never been observed for any other protein within one of the largest protein superfamily – alpha/beta hydrolases. The structure could also not be predicted. Across 12 distinct crystal forms a flexible dimer interface formed by two anti-parallel helices is observed. A PhD student in the laboratory Xiangyan You examined FphE via Small-angle X-ray scattering (SAXS) and showed that the crystal structure represents the in-solution structure. The structural aspects were then combined with efforts from our collaborators at the Stanford Bogyo laboratory. They demonstrated that the dimer influences enzymatic activity and interaction with FphE specific diagnostic probes. Combined these results show the dynamic dimer FphE to be important for future efforts to target this protein in Staphylococcus aureus. It remains to be seen if other proteins within the superfamily are also able to form this structural arrangement with implications into many research fields as alpha/beta hydrolases are used in industry to cleave molecules while also being important for all aspects of life as we know it.