4U64

Structure of the periplasmic output domain of the Legionella pneumophila LapD ortholog CdgS9 in the apo state

4U64 の概要

• エントリーDOI: 10.2210/pdb4u64/pdb
• 関連するPDBエントリー: 4U65
• 分子名称: Two component histidine kinase, GGDEF domain protein/EAL domain protein (2 entities in total)
• 機能のキーワード: signalling, pas-like fold, transferase
• 由来する生物種: Legionella pneumophila subsp. pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15118.33

構造登録者

Chatterjee, D.,Cooley, R.B.,Boyd, C.D.,Mehl, R.A.,O'Toole, G.A.,Sondermann, H.S. (登録日: 2014-07-27, 公開日: 2014-08-13, 最終更新日: 2024-10-23)

主引用文献

Chatterjee, D.,Cooley, R.B.,Boyd, C.D.,Mehl, R.A.,O'Toole, G.A.,Sondermann, H.
Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP.
Elife, 3:e03650-e03650, 2014

PubMed Abstract: Stable surface adhesion of cells is one of the early pivotal steps in bacterial biofilm formation, a prevalent adaptation strategy in response to changing environments. In Pseudomonas fluorescens, this process is regulated by the Lap system and the second messenger cyclic-di-GMP. High cytoplasmic levels of cyclic-di-GMP activate the transmembrane receptor LapD that in turn recruits the periplasmic protease LapG, preventing it from cleaving a cell surface-bound adhesin, thereby promoting cell adhesion. In this study, we elucidate the molecular basis of LapG regulation by LapD and reveal a remarkably sensitive switching mechanism that is controlled by LapD's HAMP domain. LapD appears to act as a coincidence detector, whereby a weak interaction of LapG with LapD transmits a transient outside-in signal that is reinforced only when cyclic-di-GMP levels increase. Given the conservation of key elements of this receptor system in many bacterial species, the results are broadly relevant for cyclic-di-GMP- and HAMP domain-regulated transmembrane signaling.

PubMed: 25182848
DOI: 10.7554/eLife.03650

実験手法

X-RAY DIFFRACTION (2.141 Å)