6LL5

Crystal structure of KpFtsZ (residues 11-316)

6LL5 の概要

• エントリーDOI: 10.2210/pdb6ll5/pdb
• 分子名称: Cell division protein FtsZ, GUANOSINE-5'-DIPHOSPHATE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: cell dividsion, klebsiella pneumonie, cell cycle
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32348.40

構造登録者

Yoshizawa, T.,Fujita, J.,Terakado, H.,Ozawa, M.,Kuroda, N.,Tanaka, S.,Uehara, R.,Matsumura, H. (登録日: 2019-12-21, 公開日: 2020-02-26, 最終更新日: 2023-11-22)

主引用文献

Yoshizawa, T.,Fujita, J.,Terakado, H.,Ozawa, M.,Kuroda, N.,Tanaka, S.I.,Uehara, R.,Matsumura, H.
Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli.
Acta Crystallogr.,Sect.F, 76:86-93, 2020

PubMed Abstract: FtsZ, a tubulin-like GTPase, is essential for bacterial cell division. In the presence of GTP, FtsZ polymerizes into filamentous structures, which are key to generating force in cell division. However, the structural basis for the molecular mechanism underlying FtsZ function remains to be elucidated. In this study, crystal structures of the enzymatic domains of FtsZ from Klebsiella pneumoniae (KpFtsZ) and Escherichia coli (EcFtsZ) were determined at 1.75 and 2.50 Å resolution, respectively. Both FtsZs form straight protofilaments in the crystals, and the two structures adopted relaxed (R) conformations. The T3 loop, which is involved in GTP/GDP binding and FtsZ assembly/disassembly, adopted a unique open conformation in KpFtsZ, while the T3 loop of EcFtsZ was partially disordered. The crystal structure of EcFtsZ can explain the results from previous functional analyses using EcFtsZ mutants.

PubMed: 32039890
DOI: 10.1107/S2053230X2000076X

実験手法

X-RAY DIFFRACTION (1.75 Å)