4N8O

Crystal structure of Mycobacterial FtsX extracellular domain, bromide derivative

4N8O の概要

• エントリーDOI: 10.2210/pdb4n8o/pdb
• 関連するPDBエントリー: 4N8N
• 分子名称: Cell division protein FtsX, BROMIDE ION, POTASSIUM ION, ... (4 entities in total)
• 機能のキーワード: cell wall, membrane protein
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : P9WG19
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26404.80

構造登録者

Mavrici, D. (登録日: 2013-10-17, 公開日: 2014-05-28, 最終更新日: 2024-11-20)

主引用文献

Mavrici, D.,Marakalala, M.J.,Holton, J.M.,Prigozhin, D.M.,Gee, C.L.,Zhang, Y.J.,Rubin, E.J.,Alber, T.
Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC.
Proc.Natl.Acad.Sci.USA, 111:8037-8042, 2014

PubMed Abstract: Bacterial growth and cell division are coordinated with hydrolysis of the peptidoglycan (PG) layer of the cell wall, but the mechanisms of regulation of extracellular PG hydrolases are not well understood. Here we report the biochemical, structural, and genetic analysis of the Mycobacterium tuberculosis homolog of the transmembrane PG-hydrolase regulator, FtsX. The purified FtsX extracellular domain binds the PG peptidase Rv2190c/RipC N-terminal segment, causing a conformational change that activates the enzyme. Deletion of ftsEX and ripC caused similar phenotypes in Mycobacterium smegmatis, as expected for genes in a single pathway. The crystal structure of the FtsX extracellular domain reveals an unprecedented fold containing two lobes connected by a flexible hinge. Mutations in the hydrophobic cleft between the lobes reduce RipC binding in vitro and inhibit FtsX function in M. smegmatis. These studies suggest how FtsX recognizes RipC and support a model in which a conformational change in FtsX links the cell division apparatus with PG hydrolysis.

PubMed: 24843173
DOI: 10.1073/pnas.1321812111

実験手法

X-RAY DIFFRACTION (2.3 Å)