8T88
FphE, Staphylococcus aureus fluorophosphonate-binding serine hydrolases E, Oxadiazolone JJ004 bound
Summary for 8T88
| Entry DOI | 10.2210/pdb8t88/pdb |
| Descriptor | Fluorophosphonate-binding serine hydrolase E, methyl 2-formyl-2-[4-(undec-10-ynamido)phenyl]hydrazine-1-carboxylate, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | fphe, staphylococcus aureus, s. aureus, fluorophosphonate-binding, serine hydrolases, lipase, hydrolase |
| Biological source | Staphylococcus aureus USA300-0114 |
| Total number of polymer chains | 2 |
| Total formula weight | 63345.70 |
| Authors | Fellner, M. (deposition date: 2023-06-22, release date: 2024-03-06, Last modification date: 2024-11-13) |
| Primary citation | Jo, J.,Upadhyay, T.,Woods, E.C.,Park, K.W.,Pedowitz, N.J.,Jaworek-Korjakowska, J.,Wang, S.,Valdez, T.A.,Fellner, M.,Bogyo, M. Development of Oxadiazolone Activity-Based Probes Targeting FphE for Specific Detection of Staphylococcus aureus Infections. J.Am.Chem.Soc., 146:6880-6892, 2024 Cited by PubMed Abstract: () is a major human pathogen that is responsible for a wide range of systemic infections. Since its propensity to form biofilms poses formidable challenges for both detection and treatment, tools that can be used to specifically image biofilms are highly valuable for clinical management. Here, we describe the development of oxadiazolone-based activity-based probes to target the -specific serine hydrolase FphE. Because this enzyme lacks homologues in other bacteria, it is an ideal target for selective imaging of infections. Using X-ray crystallography, direct cell labeling, and mouse models of infection, we demonstrate that oxadiazolone-based probes enable specific labeling of bacteria through the direct covalent modification of the FphE active site serine. These results demonstrate the utility of the oxadizolone electrophile for activity-based probes and validate FphE as a target for the development of imaging contrast agents for the rapid detection of infections. PubMed: 38411555DOI: 10.1021/jacs.3c13974 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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