7PL3

Crystal structure of catalytic domain in closed conformation of LytB from Streptococcus pneumoniae

7PL3 の概要

• エントリーDOI: 10.2210/pdb7pl3/pdb
• 分子名称: Putative endo-beta-N-acetylglucosaminidase, PENTAETHYLENE GLYCOL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: glucosaminidase, peptidoglycan hydrolase, hydrolase
• 由来する生物種: Streptococcus pneumoniae R6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31387.02

構造登録者

Martinez Caballero, S.,Hermoso, J.A. (登録日: 2021-08-28, 公開日: 2022-09-07, 最終更新日: 2024-02-07)

主引用文献

Martinez-Caballero, S.,Freton, C.,Molina, R.,Bartual, S.G.,Gueguen-Chaignon, V.,Mercy, C.,Gago, F.,Mahasenan, K.V.,Munoz, I.G.,Lee, M.,Hesek, D.,Mobashery, S.,Hermoso, J.A.,Grangeasse, C.
Molecular basis of the final step of cell division in Streptococcus pneumoniae.
Cell Rep, 42:112756-112756, 2023

PubMed Abstract: Bacterial cell-wall hydrolases must be tightly regulated during bacterial cell division to prevent aberrant cell lysis and to allow final separation of viable daughter cells. In a multidisciplinary work, we disclose the molecular dialogue between the cell-wall hydrolase LytB, wall teichoic acids, and the eukaryotic-like protein kinase StkP in Streptococcus pneumoniae. After characterizing the peptidoglycan recognition mode by the catalytic domain of LytB, we further demonstrate that LytB possesses a modular organization allowing the specific binding to wall teichoic acids and to the protein kinase StkP. Structural and cellular studies notably reveal that the temporal and spatial localization of LytB is governed by the interaction between specific modules of LytB and the final PASTA domain of StkP. Our data collectively provide a comprehensive understanding of how LytB performs final separation of daughter cells and highlights the regulatory role of eukaryotic-like kinases on lytic machineries in the last step of cell division in streptococci.

PubMed: 37418323
DOI: 10.1016/j.celrep.2023.112756

実験手法

X-RAY DIFFRACTION (1.8 Å)