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J. Biol. Chem., Vol. 276, Issue 34, 31994-31999, August 24, 2001

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A New Lysozyme Fold
CRYSTAL STRUCTURE OF THE MURAMIDASE FROM STREPTOMYCES COELICOLOR AT 1.65 Å RESOLUTION^*

Astrid Rau, Tanis Hogg, Rüdiger Marquardt^§, and Rolf Hilgenfeld^¶

From the  Department of Structural Biology & Crystallography, Institute of Molecular Biotechnology, Beutenbergstrasse 11, 07745 Jena, Germany and the ^§ Department of Biotechnology, Dechema e.V., Theodor-Heuss-Allee 25, 60486 Frankfurt, Germany

Cellosyl is a bacterial muramidase from Streptomyces coelicolor. Similar to other lysozymes, the enzyme cleaves the -1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine units, but it also exhibits a -1,4-N,6-O-diacetylmuramidase activity. The latter enables Cellosyl to degrade the cell walls of Staphylococcus aureus, which are not hydrolyzed by chicken-, goose-, or bacteriophage T4-type lysozymes. The enzymatic activity and amino acid sequence of Cellosyl group it with lysozymes of the Chalaropsis type, for which no detailed structural information has been available so far. The crystal structure of Cellosyl from S. coelicolor has been determined to a resolution of 1.65 Å and refined to an R-factor of 15.2%. The enzyme is comprised of a single domain and possesses an unusual /-barrel fold. The last strand, 8, of the (/)₅₃-barrel is found to be antiparallel to strands 7 and 1. Asp-9, Asp-98, and Glu-100 are located at the active site. The structure of Cellosyl exhibits a new lysozyme fold and represents a new class of polysaccharide-hydrolyzing /-barrels.

This paper is dedicated to Professor Herbert Oelschläger on the occasion of his 80th birthday.

The atomic coordinates and the structure factors (code 1JFX) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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