High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP.

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2020-02-05

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Abstract

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.

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10.1107/s2053230x20001132

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Schumacher, Maria A, Tomoo Ohashi, Lauren Corbin and Harold P Erickson (2020). High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP. Acta crystallographica. Section F, Structural biology communications, 76(Pt 2). pp. 94–102. 10.1107/s2053230x20001132 Retrieved from https://hdl.handle.net/10161/22293.

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Scholars@Duke

Schumacher

Maria Anne Schumacher

Nanaline H. Duke Distinguished Professor of Biochemistry
Erickson

Harold Paul Erickson

James B. Duke Distinguished Professor Emeritus

Recent research has been on cytoskeleton (eukaryotes and bacteria); a skirmish to debunk the irisin story; a reinterpretation of proposed multivalent binders of the coronavirus spike protein. I have also published an ebook on "Principles of Protein-Protein Association" suitable for a course module or individual learning.


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