1pgs
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THE THREE-DIMENSIONAL STRUCTURE OF PNGASE F, A GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM
OverviewOverview
BACKGROUND: Peptide:N-glycosidase F (PNGase F) is an enzyme that catalyzes, the complete removal of N-linked oligosaccharide chains from, glycoproteins. Often called an endoglycosidase, it is more correctly, termed an amidase or glycosylasparaginase as cleavage is at the, asparagine-sugar amide linkage. The enzyme is widely used in, structure-function studies of glycoproteins. RESULTS: We have determined, the crystal structure of PNGase F at 1.8 A resolution. The protein is, folded into two domains, each with an eight-stranded antiparallel beta, jelly roll configuration similar to many viral capsid proteins and also, found, in expanded form, in lectins and several glucanases. Two potential, active site regions have been identified, both in the interdomain region, and shaped by prominent loops from one domain. Exposed aromatic residues, are a feature of one site. CONCLUSIONS: The finding that PNGase F is based, on two jelly roll domains suggests parallels with lectins and other, carbohydrate-binding proteins. These proteins either bind sugars on the, concave face of the beta-sandwich structure (aided by loops) or amongst, the loops themselves. Further analysis of the function and identification, of the catalytic site should lead to an understanding of both the, specificity of PNGase F and possibly also the recognition processes that, identify glycosylation sites on proteins.
About this StructureAbout this Structure
1PGS is a Single protein structure of sequence from Elizabethkingia meningoseptica. Active as Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase, with EC number 3.5.1.52 Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of PNGase F, a glycosylasparaginase from Flavobacterium meningosepticum., Norris GE, Stillman TJ, Anderson BF, Baker EN, Structure. 1994 Nov 15;2(11):1049-59. PMID:7881905
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