“Unraveling the resistance mechanism of the enzyme penicillin binding protein of Staphylococcus aureus by serial femtosecond crystallography at X-ray free electron lasers”

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The project focuses on using time-resolved serial crystallography (TR-SX) at X-ray free electron lasers (XFELs) and synchrotrons to investigate allosteric regulation in bacterial proteins. Specifically, it aims to study the dynamic structural changes in penicillin-binding protein 2a (PBP2a) from Staphylococcus aureus (a key enzyme in antibiotic resistance) and 1,6-Anhydro-N-acetylmuramic acid kinase (AnmK) from Pseudomonas aeruginosa (involved in cell wall recycling). By capturing molecular movies of these proteins in action, the research will provide insights into enzyme mechanisms, allosteric signal propagation, and antibiotic resistance. The results could aid in the development of novel antibiotics targeting these processes.

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Reference: 2019-T1/BMD-15552

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Participating Institutions: CSIC
 

Start and End dates: 09/01/2020 - 31/08/2024
 

PI: José M. Martín García
 

Funding Agency: