2MRW

Solution Structure of MciZ from Bacillus subtilis

2MRW の概要

• エントリーDOI: 10.2210/pdb2mrw/pdb
• NMR情報: BMRB: 25096
• 分子名称: Cell division factor (1 entity in total)
• 機能のキーワード: ftsz, cell cycle
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4785.78

構造登録者

Castellen, P.,Sforca, M.L.,Zeri, A.C.M.,Gueiros-Filho, F.J. (登録日: 2014-07-16, 公開日: 2015-03-25, 最終更新日: 2024-05-01)

主引用文献

Bisson-Filho, A.W.,Discola, K.F.,Castellen, P.,Blasios, V.,Martins, A.,Sforca, M.L.,Garcia, W.,Zeri, A.C.,Erickson, H.P.,Dessen, A.,Gueiros-Filho, F.J.
FtsZ filament capping by MciZ, a developmental regulator of bacterial division.
Proc.Natl.Acad.Sci.USA, 112:E2130-E2138, 2015

PubMed Abstract: Cytoskeletal structures are dynamically remodeled with the aid of regulatory proteins. FtsZ (filamentation temperature-sensitive Z) is the bacterial homolog of tubulin that polymerizes into rings localized to cell-division sites, and the constriction of these rings drives cytokinesis. Here we investigate the mechanism by which the Bacillus subtilis cell-division inhibitor, MciZ (mother cell inhibitor of FtsZ), blocks assembly of FtsZ. The X-ray crystal structure reveals that MciZ binds to the C-terminal polymerization interface of FtsZ, the equivalent of the minus end of tubulin. Using in vivo and in vitro assays and microscopy, we show that MciZ, at substoichiometric levels to FtsZ, causes shortening of protofilaments and blocks the assembly of higher-order FtsZ structures. The findings demonstrate an unanticipated capping-based regulatory mechanism for FtsZ.

PubMed: 25848052
DOI: 10.1073/pnas.1414242112

実験手法

SOLUTION NMR