Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C: crystallization and preliminary X-ray diffraction.
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).
Van Hecke
Kristof
K
Biomolecular Architecture and BioMacS, Chemistry Department, Katholieke Universiteit Leuven, Celestijnenlaan 200F, B-3001 Heverlee, Belgium. kristof.vanhecke@chem.kuleuven.be <kristof.vanhecke@chem.kuleuven.be>
Briers
Yves
Y
Derua
Rita
R
Waelkens
Etienne
E
Lavigne
Rob
R
Van Meervelt
Luc
L
D003460:Crystallization; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000032:analysis / Q000737:chemistry*; D017902:Podoviridae / Q000737:chemistry / Q000201:enzymology; D017434:Protein Structure, Tertiary; D017105:Pseudomonas Phages / Q000737:chemistry* / Q000201:enzymology; D014961:X-Ray Diffraction
D009238:N-Acetylmuramoyl-L-alanine Amidase