6V40

Structure of Salmonella Typhi TtsA

6V40 の概要

• エントリーDOI: 10.2210/pdb6v40/pdb
• 分子名称: PG_binding_3 domain-containing protein, 2,6-DIAMINOPIMELIC ACID, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: muramidase lysozyme-like peptidoglycan-binding, protein transport
• 由来する生物種: Salmonella typhi
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 90327.76

構造登録者

Galan, J.E.,Lara-Tejero, M. (登録日: 2019-11-27, 公開日: 2020-01-29, 最終更新日: 2023-11-15)

主引用文献

Geiger, T.,Lara-Tejero, M.,Xiong, Y.,Galan, J.E.
Mechanisms of substrate recognition by a typhoid toxin secretion-associated muramidase.
Elife, 9:-, 2020

PubMed Abstract: Typhoid toxin is a virulence factor for the bacterial pathogen Typhi, which causes typhoid fever in humans. After its synthesis by intracellular bacteria, typhoid toxin is secreted into the lumen of the -containing vacuole by a secretion mechanism strictly dependent on TtsA, a specific muramidase that facilitates toxin transport through the peptidoglycan layer. Here we show that substrate recognition by TtsA depends on a discrete domain within its carboxy terminus, which targets the enzyme to the bacterial poles to recognize YcbB-edited peptidoglycan. Comparison of the atomic structures of TtsA bound to its substrate and that of a close homolog with different specificity identified specific determinants involved in substrate recognition. Combined with structure-guided mutagenesis and in vitro and in vivo crosslinking experiments, this study provides an unprecedented view of the mechanisms by which a muramidase recognizes its peptidoglycan substrate to facilitate protein secretion.

PubMed: 31958059
DOI: 10.7554/eLife.53473

実験手法

X-RAY DIFFRACTION (2.104 Å)