2WWD

3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment

2WWD の概要

• エントリーDOI: 10.2210/pdb2wwd/pdb
• 関連するPDBエントリー: 2WW5 2WWC
• 分子名称: 1,4-BETA-N-ACETYLMURAMIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-N-acetyl-alpha-muramic acid, GLYCEROL, ... (7 entities in total)
• 機能のキーワード: hydrolase, glycosidase, choline-binding proteins
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57376.19

構造登録者

Perez-Dorado, I.,Sanles, R.,Hermoso, J.A.,Gonzalez, A.,Garcia, A.,Garcia, P.,Garcia, J.L. (登録日: 2009-10-22, 公開日: 2010-04-21, 最終更新日: 2023-12-20)

主引用文献

Perez-Dorado, I.,Gonzalez, A.,Morales, M.,Sanles, R.,Striker, W.,Vollmer, W.,Mobashery, S.,Garcia, J.L.,Martinez-Ripoll, M.,Garcia, P.,Hermoso, J.A.
Insights Into Pneumococcal Fratricide from the Crystal Structures of the Modular Killing Factor Lytc.
Nat.Struct.Mol.Biol., 17:576-, 2010

PubMed Abstract: The first structure of a pneumococcal autolysin, that of the LytC lysozyme, has been solved in ternary complex with choline and a pneumococcal peptidoglycan (PG) fragment. The active site of the hydrolase module is not fully exposed but is oriented toward the choline-binding module, which accounts for its unique in vivo features in PG hydrolysis, its activation and its regulatory mechanisms. Because of the unusual hook-shaped conformation of the multimodular protein, it is only able to hydrolyze non-cross-linked PG chains, an assertion validated by additional experiments. These results explain the activation of LytC by choline-binding protein D (CbpD) in fratricide, a competence-programmed mechanism of predation of noncompetent sister cells. The results provide the first structural insights to our knowledge into the critical and central function that LytC plays in pneumococcal virulence and explain a long-standing puzzle of how murein hydrolases can be controlled to avoid self-lysis during bacterial growth and division.

PubMed: 20400948
DOI: 10.1038/NSMB.1817

実験手法

X-RAY DIFFRACTION (2.25 Å)