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High‐resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP
Author(s) -
Schumacher Maria A.,
Ohashi Tomoo,
Corbin Lauren,
Erickson Harold P.
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20001132
Subject(s) - ftsz , treadmilling , division ring , escherichia coli , cell division , tubulin , crystallography , cytokinesis , gtp' , chemistry , gtpase , mutant , cytoskeleton , biology , biophysics , microbiology and biotechnology , biochemistry , microfilament , cell , microtubule , division (mathematics) , gene , enzyme , arithmetic , mathematics
Bacterial cytokinesis is mediated by the Z‐ring, which is formed by the prokaryotic tubulin homolog FtsZ. Recent data indicate that the Z‐ring is composed of small patches of FtsZ protofilaments that travel around the bacterial cell by treadmilling. Treadmilling involves a switch from a relaxed (R) state, favored for monomers, to a tense (T) conformation, which is favored upon association into filaments. The R conformation has been observed in numerous monomeric FtsZ crystal structures and the T conformation in Staphylococcus aureus FtsZ crystallized as assembled filaments. However, while Escherichia coli has served as a main model system for the study of the Z‐ring and the associated divisome, a structure has not yet been reported for E. coli FtsZ. To address this gap, structures were determined of the E. coli FtsZ mutant FtsZ(L178E) with GDP and GTP bound to 1.35 and 1.40 Å resolution, respectively. The E. coli FtsZ(L178E) structures both crystallized as straight filaments with subunits in the R conformation. These high‐resolution structures can be employed to facilitate experimental cell‐division studies and their interpretation in E. coli .