4V02

MinC:MinD cell division protein complex, Aquifex aeolicus

4V02 の概要

• エントリーDOI: 10.2210/pdb4v02/pdb
• 関連するPDBエントリー: 4V03
• 分子名称: SITE-DETERMINING PROTEIN, PROBABLE SEPTUM SITE-DETERMINING PROTEIN MINC, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: cell cycle, bacterial cell division, ftsz, min system
• 由来する生物種: AQUIFEX AEOLICUS; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 86608.45

構造登録者

Ghosal, D.,Lowe, J. (登録日: 2014-09-10, 公開日: 2015-01-14, 最終更新日: 2024-05-08)

主引用文献

Ghosal, D.,Trambaiolo, D.,Amos, L.A.,Lowe, J.
Mincd Cell Division Proteins Form Alternating Copolymeric Cytomotive Filaments.
Nat.Commun., 5:5341-, 2014

PubMed Abstract: During bacterial cell division, filaments of the tubulin-like protein FtsZ assemble at midcell to form the cytokinetic Z-ring. Its positioning is regulated by the oscillation of MinCDE proteins. MinC is activated by MinD through an unknown mechanism and prevents Z-ring assembly anywhere but midcell. Here, using X-ray crystallography, electron microscopy and in vivo analyses, we show that MinD activates MinC by forming a new class of alternating copolymeric filaments that show similarity to eukaryotic septin filaments. A non-polymerizing mutation in MinD causes aberrant cell division in Escherichia coli. MinCD copolymers bind to membrane, interact with FtsZ and are disassembled by MinE. Imaging a functional msfGFP-MinC fusion protein in MinE-deleted cells reveals filamentous structures. EM imaging of our reconstitution of the MinCD-FtsZ interaction on liposome surfaces reveals a plausible mechanism for regulation of FtsZ ring assembly by MinCD copolymers.

PubMed: 25500731
DOI: 10.1038/NCOMMS6341

実験手法

X-RAY DIFFRACTION (2.7 Å)