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Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C: crystallization and preliminary
Kristof Van Hecke1, Yves Briers, Rita Derua
1Biomolecular Architecture and BioMacS, Chemistry Department, Katholieke Universiteit Leuven, Celestijnenlaan 200F, B-3001 Heverlee, Belgium. kristof.vanhecke@chem.kuleuven.be <kristof.vanhecke@chem.kuleuven.be>
Abstract:
The C-terminus of gp36 of bacteriophage varphiKMV (KMV36C) functions as a particle-associated muramidase, presumably as part of the injection needle of the phiKMV genome during infection. Crystals of KMV36C were obtained by hanging-drop vapour diffusion and diffracted to a resolution of 1.6 A. The crystals belong to the cubic space group P432, with unit-cell parameters a = b = c = 102.52 A. KMV36C shows 30% sequence identity to T4 lysozyme (PDB code 1l56).
Insights
The C-terminus of bacteriophage varphiKMV (KMV36C) acts as a muramidase, likely aiding in phage genome injection. Its crystal structure was determined to 1.6 A resolution, revealing similarities to T4 lysozyme.
Area of Science:
- Structural biology
- Virology
- Biochemistry
Background:
- Bacteriophage varphiKMV (phiKMV) utilizes a particle-associated muramidase, the C-terminus of gp36 (KMV36C), for genome injection.
- Understanding the structure of KMV36C is crucial for elucidating the mechanism of bacteriophage infection.
Purpose of the Study:
- To determine the crystal structure of KMV36C.
- To provide insights into the function of KMV36C as a muramidase.
Main Methods:
- Crystallization of KMV36C using hanging-drop vapour diffusion.
- X-ray diffraction data collection to a resolution of 1.6 A.
- Analysis of crystal space group (P432) and unit-cell parameters.
Main Results:
- High-resolution crystal structure of KMV36C was obtained.
- The crystal structure belongs to the cubic space group P432 with specific unit-cell parameters.
- KMV36C exhibits 30% sequence identity to T4 lysozyme, suggesting conserved structural and functional features.
Conclusions:
- The determined structure of KMV36C provides a foundation for understanding its role in bacteriophage infection.
- Structural similarity to T4 lysozyme may indicate conserved enzymatic mechanisms or evolutionary relationships.
