2NDA

Solution structure of MapZ extracellular domain second subdomain

2NDA の概要

• エントリーDOI: 10.2210/pdb2nda/pdb
• 関連するPDBエントリー: 2ND9
• NMR情報: BMRB: 26053
• 分子名称: Mid-cell-anchored protein Z (1 entity in total)
• 機能のキーワード: mapz, ftsz, peptidoglycan, division, cell cycle
• 由来する生物種: Streptococcus pneumoniae R6 (Streptococcus pneumoniae)
• 細胞内の位置: Cell membrane ; Single-pass membrane protein : Q8DR55
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12311.38

構造登録者

Jean, N.L.,Manuse, S.,Guinot, M.,Bougault, C.M.,Grangeasse, C.,Simorre, J.-P. (登録日: 2016-05-11, 公開日: 2016-06-29, 最終更新日: 2024-05-01)

主引用文献

Manuse, S.,Jean, N.L.,Guinot, M.,Lavergne, J.P.,Laguri, C.,Bougault, C.M.,VanNieuwenhze, M.S.,Grangeasse, C.,Simorre, J.P.
Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ.
Nat Commun, 7:12071-12071, 2016

PubMed Abstract: Accurate placement of the bacterial division site is a prerequisite for the generation of two viable and identical daughter cells. In Streptococcus pneumoniae, the positive regulatory mechanism involving the membrane protein MapZ positions precisely the conserved cell division protein FtsZ at the cell centre. Here we characterize the structure of the extracellular domain of MapZ and show that it displays a bi-modular structure composed of two subdomains separated by a flexible serine-rich linker. We further demonstrate in vivo that the N-terminal subdomain serves as a pedestal for the C-terminal subdomain, which determines the ability of MapZ to mark the division site. The C-terminal subdomain displays a patch of conserved amino acids and we show that this patch defines a structural motif crucial for MapZ function. Altogether, this structure-function analysis of MapZ provides the first molecular characterization of a positive regulatory process of bacterial cell division.

PubMed: 27346279
DOI: 10.1038/ncomms12071

実験手法

SOLUTION NMR