3WGJ

STAPHYLOCOCCUS AUREUS FTSZ T7 chimera mutant, T7Bs

3WGJ の概要

• エントリーDOI: 10.2210/pdb3wgj/pdb
• 関連するPDBエントリー: 3WGK 3WGL 3WGM 3WGN 3vo8 3voa
• 分子名称: Cell division protein FtsZ, CALCIUM ION (3 entities in total)
• 機能のキーワード: ftsz, gtp-binding, tubulin homolog, polymerization, gtpase, cell division, cell cycle
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Cytoplasm (By similarity): P0A029
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63806.37

構造登録者

Matsui, T.,Tanaka, I.,Yao, M. (登録日: 2013-08-06, 公開日: 2013-12-25, 最終更新日: 2023-11-08)

主引用文献

Matsui, T.,Han, X.,Yu, J.,Yao, M.,Tanaka, I.
Structural change in FtsZ Induced by intermolecular interactions between bound GTP and the T7 loop
J.Biol.Chem., 289:3501-3509, 2014

PubMed Abstract: FtsZ is a prokaryotic homolog of tubulin and is a key molecule in bacterial cell division. FtsZ with bound GTP polymerizes into tubulin-like protofilaments. Upon polymerization, the T7 loop of one subunit is inserted into the nucleotide-binding pocket of the second subunit, which results in GTP hydrolysis. Thus, the T7 loop is important for both polymerization and hydrolysis in the tubulin/FtsZ family. Although x-ray crystallography revealed both straight and curved conformations of tubulin, only a curved structure was known for FtsZ. Recently, however, FtsZ from Staphylococcus aureus has been shown to have a very different conformation from the canonical FtsZ structure. The present study was performed to investigate the structure of FtsZ from Staphylococcus aureus by mutagenesis experiments; the effects of amino acid changes in the T7 loop on the structure as well as on GTPase activity were studied. These analyses indicated that FtsZ changes its conformation suitable for polymerization and GTP hydrolysis by movement between N- and C-subdomains via intermolecular interactions between bound nucleotide and residues in the T7 loop.

PubMed: 24347164
DOI: 10.1074/jbc.M113.514901

実験手法

X-RAY DIFFRACTION (2.179 Å)