1jfx: Difference between revisions
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|PDB= 1jfx |SIZE=350|CAPTION= <scene name='initialview01'>1jfx</scene>, resolution 1.65Å | |PDB= 1jfx |SIZE=350|CAPTION= <scene name='initialview01'>1jfx</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= cel ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 Streptomyces coelicolor]) | |GENE= cel ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 Streptomyces coelicolor]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jfx OCA], [http://www.ebi.ac.uk/pdbsum/1jfx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jfx RCSB]</span> | |||
}} | }} | ||
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[[Category: Marquardt, R.]] | [[Category: Marquardt, R.]] | ||
[[Category: Rau, A.]] | [[Category: Rau, A.]] | ||
[[Category: beta-alpha-barrel]] | [[Category: beta-alpha-barrel]] | ||
[[Category: cellosyl]] | [[Category: cellosyl]] | ||
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[[Category: n-acetylmuramidase]] | [[Category: n-acetylmuramidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:33:06 2008'' | ||
Revision as of 21:33, 30 March 2008
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| , resolution 1.65Å | |||||||
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| Ligands: | |||||||
| Gene: | cel (Streptomyces coelicolor) | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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