The FtsZ dimer was studied to gain insights into FtsZ protofilament formation. In the simulation study of the dimer it was found that the monomer-monomer contacts in the GDP bound dimer is lower which results in the high curvature of the GDP bound protofilaments. In this study, the FtsZ dimer was simulated.
View Article and Find Full Text PDFEarlier molecular dynamics studies of the FtsZ protein revealed that the protein has high intrinsic flexibility which the crystal structures cannot reveal. However, the input structure in these simulation studies was based on the available crystal structure data and therefore, the effect of the C-terminal Intrinsically Disordered Region (IDR) of FtsZ could not be observed in any of these studies. Recent investigations have revealed that the C-terminal IDR is crucial for FtsZ assembly and Z ring formation .
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