6H5F

LtgA disordered Helix

「4YP4」から置き換えられました

6H5F の概要

• エントリーDOI: 10.2210/pdb6h5f/pdb
• 分子名称: Putative soluble lytic murein transglycosylase (2 entities in total)
• 機能のキーワード: peptidoglycan, antibiotic resistance, enzyme hub, transferase
• 由来する生物種: Neisseria meningitidis NM422
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67824.35

構造登録者

Williams, A.H. (登録日: 2018-07-24, 公開日: 2019-08-28, 最終更新日: 2024-11-13)

主引用文献

Williams, A.H.,Wheeler, R.,Deghmane, A.E.,Santecchia, I.,Schaub, R.E.,Hicham, S.,Moya Nilges, M.,Malosse, C.,Chamot-Rooke, J.,Haouz, A.,Dillard, J.P.,Robins, W.P.,Taha, M.K.,Gomperts Boneca, I.
Defective lytic transglycosylase disrupts cell morphogenesis by hindering cell wall de-O-acetylation inNeisseria meningitidis.
Elife, 9:-, 2020

PubMed Abstract: Lytic transglycosylases (LT) are enzymes involved in peptidoglycan (PG) remodeling. However, their contribution to cell-wall-modifying complexes and their potential as antimicrobial drug targets remains unclear. Here, we determined a high-resolution structure of the LT, an outer membrane lipoprotein from species with a disordered active site helix (alpha helix 30). We show that deletion of the conserved alpha-helix 30 interferes with the integrity of the cell wall, disrupts cell division, cell separation, and impairs the fitness of the human pathogen during infection. Additionally, deletion of alpha-helix 30 results in hyperacetylated PG, suggesting this LtgA variant affects the function of the PG de-acetylase (Ape 1). Our study revealed that Ape 1 requires LtgA for optimal function, demonstrating that LTs can modulate the activity of their protein-binding partner. We show that targeting specific domains in LTs can be lethal, which opens the possibility that LTs are useful drug-targets.

PubMed: 32022687
DOI: 10.7554/eLife.51247

実験手法

X-RAY DIFFRACTION (2 Å)