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Literature DB >> 18391422

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

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

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).

Entities: Disease Species

Mesh：

Substances：

Year: 2008 PMID： 18391422 PMCID： PMC2374246 DOI： 10.1107/S1744309108004569

Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091

11 in total

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