7BBA

Structure of the TagL peptidoglycan binding domain from EAEC T6SS

「5M3G」から置き換えられました

7BBA の概要

• エントリーDOI: 10.2210/pdb7bba/pdb
• 分子名称: Putative type VI secretion protein, SULFATE ION (3 entities in total)
• 機能のキーワード: peptidoglycan binding protein, type vi secretion system, protein binding
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 61384.77

構造登録者

Nguyen, V.S.,Cambillau, C.,Leone, P. (登録日: 2020-12-17, 公開日: 2021-08-04, 最終更新日: 2024-01-31)

主引用文献

Nguyen, V.S.,Spinelli, S.,Cascales, E.,Roussel, A.,Cambillau, C.,Leone, P.
Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.
Plos One, 16:e0254232-e0254232, 2021

PubMed Abstract: The type VI secretion system (T6SS) is a widespread mechanism of protein delivery into target cells, present in more than a quarter of all sequenced Gram-negative bacteria. The T6SS constitutes an important virulence factor, as it is responsible for targeting effectors in both prokaryotic and eukaryotic cells. The T6SS comprises a tail structure tethered to the cell envelope via a trans-envelope complex. In most T6SS, the membrane complex is anchored to the cell wall by the TagL accessory protein. In this study, we report the first crystal structure of a peptidoglycan-binding domain of TagL. The fold is conserved with members of the OmpA/Pal/MotB family, and more importantly, the peptidoglycan binding site is conserved. This structure further exemplifies how proteins involved in anchoring to the cell wall for different cellular functions rely on an interaction network with peptidoglycan strictly conserved.

PubMed: 34214145
DOI: 10.1371/journal.pone.0254232

実験手法

X-RAY DIFFRACTION (2.43 Å)