What is it about?
FtsZ is a cellular machine whose dynamic properties allow bacterial division, an essential step in the progression of infections. FtsZ self-assembles forming single filaments that hydrolyze the energy-rich nucleotide GTP. GTP hydrolysis fuels these filaments to grow and shrink simultaneously at opposite ends, causing a translocation movement similar to that of a treadmill. In association with other proteins, dynamic FtsZ filaments form a ring that allows the remodeling of the bacterial cell wall, finally leading to cell division. Because bacterial division is essential for the dissemination of infections, this process is a target for the discovery of new antibiotics. Ruiz et al. present the high-resolution structures obtained by X-ray crystallography of FtsZ filaments from methicillin-resistant Staphylococcus aureus (MRSA) in complex with different cations and nucleotide analogs, including those that mimic the ground and transition states of GTP hydrolysis. Combined with mutational and biochemical analysis, the structures allowed identification of key FtsZ amino acids involved in GTP hydrolysis. The structures provide atomic details of the process by which FtsZ coordinates GTP hydrolysis with conformational changes essential for FtsZ filament treadmilling.
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Why is it important?
Antibiotic resistance causes more than one million deaths a year worldwide and it is estimated that this figure could increase tenfold in the coming decades. About one-tenth of current deaths are due to infections caused by MRSA infections alone. The FtsZ protein of this pathogen, subject of the study, plays a central role in cell division necessary for the spread of these infections. Providing insight into the intimate mechanisms of bacterial cell division paves the way for biomedical applications.
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This page is a summary of: FtsZ filament structures in different nucleotide states reveal the mechanism of assembly dynamics, PLoS Biology, March 2022, PLOS,
DOI: 10.1371/journal.pbio.3001497.
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