2e32
Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase
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OverviewOverview
The ubiquitin ligase complex SCF(Fbs1), which contributes to the, ubiquitination of glycoproteins, is involved in the endoplasmic, reticulum-associated degradation pathway. In SCF ubiquitin ligases, a, diverse array of F-box proteins confers substrate specificity. Fbs1/Fbx2, a member of the F-box protein family, recognizes high-mannose, oligosaccharides. To elucidate the structural basis of SCF(Fbs1) function, we determined the crystal structures of the Skp1-Fbs1 complex and the, sugar-binding domain (SBD) of the Fbs1-glycoprotein complex. The, mechanistic model indicated by the structures appears to be well conserved, among the SCF ubiquitin ligases. The structure of the SBD-glycoprotein, complex indicates that the SBD primarily recognizes Man(3)GlcNAc(2), thereby explaining the broad activity of the enzyme against various, glycoproteins. Comparison of two crystal structures of the Skp1-Fbs1, complex revealed the relative motion of a linker segment between the F-box, and the SBD domains, which might underlie the ability of the complex to, recognize different acceptor lysine residues for ubiquitination.
About this StructureAbout this Structure
2E32 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the selection of glycosylated substrates by SCFFbs1 ubiquitin ligase., Mizushima T, Yoshida Y, Kumanomidou T, Hasegawa Y, Suzuki A, Yamane T, Tanaka K, Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5777-81. Epub 2007 Mar 26. PMID:17389369
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