6UNX

Structure of E. coli FtsZ(L178E)-GTP complex

6UNX の概要

• エントリーDOI: 10.2210/pdb6unx/pdb
• 分子名称: Cell division protein FtsZ, GUANOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: ftsz, cell division, divisive, cell cycle
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34443.48

構造登録者

Schumacher, M.A. (登録日: 2019-10-13, 公開日: 2020-02-05, 最終更新日: 2023-10-11)

主引用文献

Schumacher, M.A.,Ohashi, T.,Corbin, L.,Erickson, H.P.
High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP.
Acta Crystallogr.,Sect.F, 76:94-102, 2020

PubMed 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.

PubMed: 32039891
DOI: 10.1107/S2053230X20001132

実験手法

X-RAY DIFFRACTION (1.4 Å)