1y4j
Crystal structure of the paralogue of the human formylglycine generating enzyme
|
OverviewOverview
In eukaryotes, sulfate esters are degraded by sulfatases, which possess a, unique Calpha-formylglycine residue in their active site. The defect in, post-translational formation of the Calpha-formylglycine residue causes a, severe lysosomal storage disorder in humans. Recently, FGE, (formylglycine-generating enzyme) has been identified as the protein, required for this specific modification. Using sequence comparisons, a, protein homologous to FGE was found and denoted pFGE (paralog of FGE)., pFGE binds a sulfatase-derived peptide bearing the FGE recognition motif, but it lacks formylglycine-generating activity. Both proteins belong to a, large family of pro- and eukaryotic proteins containing the DUF323 domain, a formylglycine-generating enzyme domain of unknown three-dimensional, structure. We have crystallized the glycosylated human pFGE and determined, its crystal structure at a resolution of 1.86 A. The structure reveals a, novel fold, which we denote the FGE fold and which therefore serves as a, paradigm for the DUF323 domain. It is characterized by an asymmetric, partitioning of secondary structure elements and is stabilized by two, calcium cations. A deep cleft on the surface of pFGE most likely, represents the sulfatase polypeptide binding site. The asymmetric unit of, the pFGE crystal contains a homodimer. The putative peptide binding site, is buried between the monomers, indicating a biological significance of, the dimer. The structure suggests the capability of pFGE to form a, heterodimer with FGE.
About this StructureAbout this Structure
1Y4J is a Single protein structure of sequence from Homo sapiens with CA and MPD as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme., Dickmanns A, Schmidt B, Rudolph MG, Mariappan M, Dierks T, von Figura K, Ficner R, J Biol Chem. 2005 Apr 15;280(15):15180-7. Epub 2005 Feb 1. PMID:15687489
Page seeded by OCA on Mon Nov 12 20:14:47 2007