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Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1
Juan A Hermoso1, Begoña Monterroso, Armando Albert
1Grupo de Cristalografía Macromolecular y Biología Estructural, de Macromoléculas Biológicas, Instituto Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain. xjuan@iqfr.csic.es
Structure (London, England : 1993)
|October 7, 2003
Summary
Pneumococcal bacteriophage lysins, or enzybiotics, show promise against streptococcal infections. This study reveals the Cpl-1 lysin structure, detailing its catalytic and choline binding modules for potential therapeutic applications.
Area of Science:
- Structural biology
- Microbiology
- Biochemistry
Background:
- Pneumococcal bacteriophage lysins are modular proteins acting as enzybiotics.
- These proteins target streptococcal infections by degrading bacterial cell walls.
Purpose of the Study:
- To determine the crystal structures of the Cpl-1 lysin in free and choline-bound states.
- To elucidate the catalytic mechanism of glycoside hydrolase family 25.
- To understand the role of choline binding repeats (ChBrs) in protein structure and function.
Main Methods:
- X-ray crystallography
- Site-directed mutagenesis
- Structural analysis of protein domains
Main Results:
- The crystal structures of free and choline-bound Cpl-1 lysin were determined.
- The catalytic module features an irregular (beta/alpha)(5)beta(3) barrel.
- The cell wall-anchoring module consists of six ChBrs forming a superhelical domain and a beta sheet domain.
Conclusions:
- The study provides the first complete structure of a choline binding protein.
- A general catalytic mechanism for glycoside hydrolase family 25 is proposed.
- Choline binding repeats are versatile elements influencing protein evolution and specificity.