McCoy, Kelsey M., Keith J. Fritzsching, and Ann E. McDermott. “GTP-Bound Escherichia Coli FtsZ Filaments Are Composed of Tense Monomers: A Dynamic Nuclear Polarization-Nuclear Magnetic Resonance Study Using Interface Detection.” Edited by Indranil Biswas. MBio, October 10, 2022, e02358-22.
https://doi.org/10.1128/mbio.02358-22.
FtsZ filaments are the major structural component of the bacterial Z ring and are drivers of bacterial division. Crystal structures for FtsZ from some Grampositive bacteria in the presence of GTP analogs suggest the possibility of a highenergy, “tense” conformation. It remains important to elucidate whether this tense form is the dominant form in filaments. Using dynamic nuclear polarization (DNP) solid-state nuclear magnetic resonance (NMR) and differential isotopic labeling, we directly detected residues located at the intermonomer interface of GTP-bound wildtype (WT) Escherichia coli FtsZ filaments. We combined chemical shift prediction, homology modeling, and heteronuclear dipolar recoupling techniques to characterize the E. coli FtsZ filament interface and demonstrated that the monomers in active filaments assume a tense conformation.