5NR1

FzlA from C. crescentus

5NR1 の概要

• エントリーDOI: 10.2210/pdb5nr1/pdb
• 分子名称: FtsZ-binding protein FzlA (2 entities in total)
• 機能のキーワード: bacterial cell division, ftsz, cell cycle
• 由来する生物種: Caulobacter crescentus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26613.72

構造登録者

Szwedziak, P.,Lowe, J. (登録日: 2017-04-21, 公開日: 2017-06-07, 最終更新日: 2024-05-08)

主引用文献

Lariviere, P.J.,Szwedziak, P.,Mahone, C.R.,Lowe, J.,Goley, E.D.
FzlA, an essential regulator of FtsZ filament curvature, controls constriction rate during Caulobacter division.
Mol. Microbiol., 107:180-197, 2018

PubMed Abstract: During bacterial division, polymers of the tubulin-like GTPase FtsZ assemble at midcell to form the cytokinetic Z-ring, which coordinates peptidoglycan (PG) remodeling and envelope constriction. Curvature of FtsZ filaments promotes membrane deformation in vitro, but its role in division in vivo remains undefined. Inside cells, FtsZ directs PG insertion at the division plane, though it is unclear how FtsZ structure and dynamics are mechanistically coupled to PG metabolism. Here we study FzlA, a division protein that stabilizes highly curved FtsZ filaments, as a tool for assessing the contribution of FtsZ filament curvature to constriction. We show that in Caulobacter crescentus, FzlA must bind to FtsZ for division to occur and that FzlA-mediated FtsZ curvature is correlated with efficient division. We observed that FzlA influences constriction rate, and that this activity is associated with its ability to bind and curve FtsZ polymers. Further, we found that a slowly constricting fzlA mutant strain develops 'pointy' poles, suggesting that FzlA influences the relative contributions of radial versus longitudinal PG insertion at the septum. These findings implicate FzlA as a critical coordinator of envelope constriction through its interaction with FtsZ and suggest a functional link between FtsZ curvature and efficient constriction in C. crescentus.

PubMed: 29119622
DOI: 10.1111/mmi.13876

実験手法

X-RAY DIFFRACTION (2.004 Å)