3VO8

Staphylococcus aureus FtsZ GDP-form

3VO8 の概要

• エントリーDOI: 10.2210/pdb3vo8/pdb
• 関連するPDBエントリー: 3VO9 3VOA 3VOB
• 分子名称: Cell division protein FtsZ, CALCIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 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: 83514.57

構造登録者

Matsui, T.,Mogi, N.,Yao, M.,Tanaka, I. (登録日: 2012-01-20, 公開日: 2012-08-29, 最終更新日: 2023-11-08)

主引用文献

Matsui, T.,Yamane, J.,Mogi, N.,Yamaguchi, H.,Takemoto, H.,Yao, M.,Tanaka, I.
Structural reorganization of the bacterial cell-division protein FtsZ from Staphylococcus aureus
Acta Crystallogr.,Sect.D, 68:1175-1188, 2012

PubMed Abstract: FtsZ is a key molecule in bacterial cell division. In the presence of GTP, it polymerizes into tubulin-like protofilaments by head-to-tail association. Protofilaments of FtsZ seem to adopt a straight or a curved conformation in relation to the bound nucleotide. However, although several bacterial and archaeal FtsZ structures have been determined, all of the structures reported previously are considered to have a curved conformation. In this study, structures of FtsZ from Staphylococcus aureus (SaFtsZ) were determined in apo, GDP-bound and inhibitor-complex forms and it was found that SaFtsZ undergoes marked conformational changes. The accumulated evidence suggests that the GDP-bound structure has the features of the straight form. The structural change between the curved and straight forms shows intriguing similarity to the eukaryotic cytoskeletal protein tubulin. Furthermore, the structure of the apo form showed an unexpectedly large conformational change in the core region. FtsZ has also been recognized as a novel target for antibacterial drugs. The structure of the complex with the inhibitor PC190723, which has potent and selective antistaphylococcal activity, indicated that the inhibitor binds at the cleft between the two subdomains.

PubMed: 22948918
DOI: 10.1107/S0907444912022640

実験手法

X-RAY DIFFRACTION (2.255 Å)