Crystal structure of the bacterial cell-division protein FtsZ

By J. Löwe, L. Amos. 1998

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Protein Sequence Analysis Using the MPI Bioinformatics Toolkit (2020, background): “…all chloroplasts, and some mitochondria, with the latter two representing endosymbiosis-derived eukaryotic organelles, FtsZ forms filaments that assemble into a ring (Z-ring) at the future site of cell division (Lowe & Amos, 1998; Margolin, 2005; Szwedziak, Wang, Bharat, Tsim, & Lowe, 2014).”
Bacterial cell division: assembly, maintenance and disassembly of the Z ring (2009, result): “Despite the low level of sequence similarity, the tertiary structure of FtsZ is remarkably similar to that of tubulin, supporting the theory that these proteins have common ancestr”
Mechanisms of Taxol resistance related to microtubules (2003, unknown): “%) to tubulin (Lowe and Amos, 1998).”
FtsZ and the division of prokaryotic cells and organelles (2005, background): “FtsZ contains four main protein domains, as determined by the crystal structure of FtsZ from the thermophilic bacterium Thermotoga maritima”
Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain (2004, background): “One possibility is that binding of GTP to the tubulin β subunit results in a conformational change that locks the H7 lever heli”