Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C: crystallization and preliminary X-ray diffraction

Kristof Van Hecke; Yves Briers; Rita Derua; Etienne Waelkens; Rob Lavigne; Luc Van Meervelt

doi:10.1107/S1744309108004569

Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C: crystallization and preliminary X-ray diffraction

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt 4):263-5. doi: 10.1107/S1744309108004569. Epub 2008 Mar 21.

Authors

Kristof Van Hecke¹, Yves Briers, Rita Derua, Etienne Waelkens, Rob Lavigne, Luc Van Meervelt

Affiliation

¹ Biomolecular Architecture and BioMacS, Chemistry Department, Katholieke Universiteit Leuven, Celestijnenlaan 200F, B-3001 Heverlee, Belgium. [email protected] <[email protected]>

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).

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
N-Acetylmuramoyl-L-alanine Amidase / analysis
N-Acetylmuramoyl-L-alanine Amidase / chemistry*
Podoviridae / chemistry
Podoviridae / enzymology
Protein Structure, Tertiary
Pseudomonas Phages / chemistry*
Pseudomonas Phages / enzymology
X-Ray Diffraction

Substances

N-Acetylmuramoyl-L-alanine Amidase