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. The initial structure was obtained from our previous study in which we had simulated the FtsZ monomer with its C-terminal IDR (Intrinsically Disordered Region). The FtsZ dimer subunit contacts were used as the starting configuration. Simulations of the dimer were performed with GTP and with GDP. It is found that the central helix H5 closes by about 15 degrees in the simulation with GTP than in the simulation with GDP. The C-terminal IDR and the C-terminal domain region between SC2 and HC2 are found to have much high flexibility and hence exhibit domain motion.Communicated by Ramaswamy H. Sarma.
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http://dx.doi.org/10.1080/07391102.2023.2287486 | DOI Listing |
Anal Biochem
January 2025
Laboratorio de Biología Estructural y Molecular BEM, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425 Ñuñoa, Santiago, 7800003, Chile; Laboratorio de Biotecnología Vegetal y Ambiental Aplicada, Universidad Tecnológica Metropolitana, Santiago, Chile.
FtsZ is a bacterial protein that plays a crucial role in cytokinesis by forming the Z-ring. This ring acts as a scaffold to recruit other division proteins and guide the synthesis of septal peptidoglycan, which leads to cell constriction. In its native state, the FtsZ protein from Escherichia coli (EcFtsZ) is a multi-oligomer comprising dimers, trimers, tetramers, and hexamers in a dynamic self-association equilibrium depending on its concentration.
View Article and Find Full Text PDFCytoskeleton (Hoboken)
December 2024
GN Ramachandran Protein Center, CSIR Institute of Microbial Technology, Chandigarh, India.
Z-ring formation by FtsZ, the master assembler of the divisome, is a key step in bacterial cell division. Membrane anchoring of the Z-ring requires the assistance of dedicated Z-ring binding proteins, such as SepF and FtsA. SepF participates in bundling and membrane anchoring of FtsZ in gram-positive bacteria.
View Article and Find Full Text PDFbioRxiv
December 2024
Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306.
CrgA is a key transmembrane (TM) protein in the cell division process of (), the pathogen responsible for tuberculosis. While many of the divisome proteins have been identified, their structures and interactions remain largely unknown. Previous studies of CrgA using oriented-sample solid-state NMR have defined the tilt and rotation of the TM helices, but the cytoplasmic and periplasmic domains and even the oligomeric state were uncharacterized.
View Article and Find Full Text PDFMol Biol Cell
October 2024
Biophysics Program, Stanford University, Stanford, CA 94305.
The key bacterial cell division protein FtsZ can adopt multiple conformations, and prevailing models suggest that transitions of FtsZ subunits from the closed to open state are necessary for filament formation and stability. Using all-atom molecular dynamics simulations, we analyzed state transitions of FtsZ as a monomer, dimer, and hexamer. We found that monomers can adopt intermediate states but preferentially adopt a closed state that is robust to forced reopening.
View Article and Find Full Text PDFJ Biol Chem
June 2024
Biology Division, Indian Institute of Science Education and Research, Pune, India. Electronic address:
FtsZ, the tubulin homolog essential for bacterial cell division, assembles as the Z-ring at the division site, and directs peptidoglycan synthesis by treadmilling. It is unclear how FtsZ achieves kinetic polarity that drives treadmilling. To obtain insights into fundamental features of FtsZ assembly dynamics independent of peptidoglycan synthesis, we carried out structural and biochemical characterization of FtsZ from the cell wall-less bacteria, Spiroplasma melliferum (SmFtsZ).
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