8BZ5

Crystal structure of the L. monocytogenes RmlT in complex with HEPES

8BZ5 の概要

• エントリーDOI: 10.2210/pdb8bz5/pdb
• 関連するPDBエントリー: 8BZ4 8BZ6 8BZ7 8BZ8
• 分子名称: Glycosyltransferase, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (3 entities in total)
• 機能のキーワード: glycosyltransferase, transferase
• 由来する生物種: Listeria monocytogenes
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 290841.21

構造登録者

Cereija, T.B.,Morais-Cabral, J.H. (登録日: 2022-12-14, 公開日: 2023-12-27, 最終更新日: 2025-02-05)

主引用文献

Monteiro, R.,Cereija, T.B.,Pombinho, R.,Voskuilen, T.,Codee, J.D.C.,Sousa, S.,Morais-Cabral, J.H.,Cabanes, D.
Molecular properties of the RmlT wall teichoic acid rhamnosyltransferase that modulates virulence in Listeria monocytogenes.
Nat Commun, 16:24-24, 2025

PubMed Abstract: Wall teichoic acids (WTAs) from the major Gram-positive foodborne pathogen Listeria monocytogenes are peptidoglycan-associated glycopolymers decorated by monosaccharides that, while not essential for bacterial growth, are required for bacterial virulence and resistance to antimicrobials. Here we report the structure and function of a bacterial WTAs rhamnosyltransferase, RmlT, strictly required for L. monocytogenes WTAs rhamnosylation. In particular, we demonstrated that RmlT transfers rhamnose from dTDP-L-rhamnose to naked WTAs, and that specificity towards TDP-rhamnose is not determined by its binding affinity. Structures of RmlT with and without its substrates showed that this enzyme is a dimer, revealed the residues responsible for interaction with the substrates and that the catalytic residue pre-orients the acceptor substrate towards the nucleophilic attack to the sugar. Additionally, the structures provided indications for two potential interaction pathways for the long WTAs on the surface of RmlT. Finally, we confirmed that WTAs glycosyltransferases are promising targets for next-generation strategies against Gram-positive pathogens by showing that inactivation of the RmlT catalytic activity results in a decreased infection in vivo.

PubMed: 39746981
DOI: 10.1038/s41467-024-55360-1

実験手法

X-RAY DIFFRACTION (2.3 Å)