1jfx: Difference between revisions

Revision as of 14:22, 21 February 2008

Crystal structure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution

OverviewOverview

Cellosyl is a bacterial muramidase from Streptomyces coelicolor. Similar to other lysozymes, the enzyme cleaves the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine units, but it also exhibits a beta-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 A and refined to an R-factor of 15.2%. The enzyme is comprised of a single domain and possesses an unusual beta/alpha-barrel fold. The last strand, beta 8, of the (beta/alpha)(5)beta(3)-barrel is found to be antiparallel to strands beta 7 and beta 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 beta/alpha-barrels.

About this StructureAbout this Structure

1JFX is a Single protein structure of sequence from Streptomyces coelicolor with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 A resolution., Rau A, Hogg T, Marquardt R, Hilgenfeld R, J Biol Chem. 2001 Aug 24;276(34):31994-9. Epub 2001 Jun 26. PMID:11427528

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-[[Image:1jfx.jpg|left|200px]]<br /><applet load="1jfx" size="450" color="white" frame="true" align="right" spinBox="true"
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 '''Crystal structure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution'''<br />
 ==Overview==
-Cellosyl is a bacterial muramidase from Streptomyces coelicolor. Similar, to other lysozymes, the enzyme cleaves the beta-1,4-glycosidic bond, between N-acetylmuramic acid and N-acetylglucosamine units, but it also, exhibits a beta-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 A and, refined to an R-factor of 15.2%. The enzyme is comprised of a single, domain and possesses an unusual beta/alpha-barrel fold. The last strand, beta 8, of the (beta/alpha)(5)beta(3)-barrel is found to be antiparallel, to strands beta 7 and beta 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, beta/alpha-barrels.
+Cellosyl is a bacterial muramidase from Streptomyces coelicolor. Similar to other lysozymes, the enzyme cleaves the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine units, but it also exhibits a beta-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 A and refined to an R-factor of 15.2%. The enzyme is comprised of a single domain and possesses an unusual beta/alpha-barrel fold. The last strand, beta 8, of the (beta/alpha)(5)beta(3)-barrel is found to be antiparallel to strands beta 7 and beta 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 beta/alpha-barrels.
 ==About this Structure==
-JFX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JFX OCA].
+JFX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JFX OCA].
 ==Reference==
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 [[Category: n-acetylmuramidase]]
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