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2MMV

ZapA mutant dimer from Geobacillus stearothermophilus

2MMV の概要
エントリーDOI10.2210/pdb2mmv/pdb
NMR情報BMRB: 19869
分子名称Cell division protein ZapA (1 entity in total)
機能のキーワードzapa, cell cycle
由来する生物種Geobacillus stearothermophilus
細胞内の位置Cytoplasm : A0A078N0N2
タンパク質・核酸の鎖数2
化学式量合計19804.86
構造登録者
Nogueira, M.L.,Sforca, M.,Zeri, A. (登録日: 2014-03-19, 公開日: 2015-06-17, 最終更新日: 2024-05-15)
主引用文献Nogueira, M.L.,Sforca, M.L.,Chin, Y.K.,Mobli, M.,Handler, A.,Gorbatyuk, V.Y.,Robson, S.A.,King, G.F.,Gueiros-Filho, F.J.,Zeri, A.C.
Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ.
Biomol.Nmr Assign., 9:387-391, 2015
Cited by
PubMed Abstract: Bacterial division begins with the formation of a contractile protein ring at midcell, which constricts the bacterial envelope to generate two daughter cells. The central component of the division ring is FtsZ, a tubulin-like protein capable of self-assembling into filaments which further associate into a higher order structure known as the Z ring. Proteins that bind to FtsZ play a crucial role in the formation and regulation of the Z ring. One such protein is ZapA, a widely conserved 21 kDa homodimeric protein that associates with FtsZ filaments and promotes their bundling. Although ZapA was discovered more than a decade ago, the structural details of its interaction with FtsZ remain unknown. In this work, backbone and side chain NMR assignments for the Geobacillus stearothermophilus ZapA homodimer are described. We titrated FtsZ into (15)N(2)H-ZapA and mapped ZapA residues whose resonances are perturbed upon FtsZ binding. This information provides a structural understanding of the interaction between FtsZ and ZapA.
PubMed: 25967379
DOI: 10.1007/s12104-015-9615-1
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2mmv
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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