2E32

Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase

Summary for 2E32

• Entry DOI: 10.2210/pdb2e32/pdb
• Related: 2E31 2E33
• Descriptor: F-box only protein 2, S-phase kinase-associated protein 1A (2 entities in total)
• Functional Keywords: ubiquitin, scf, ubiquitin ligase, fbs1, ligase
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cytoplasm: Q80UW2
• Total number of polymer chains: 4
• Total formula weight: 105298.08

Authors

Mizushima, T.,Yoshida, Y.,Kumanomidou, T.,Hasegawa, Y.,Yamane, T.,Tanaka, K. (deposition date: 2006-11-20, release date: 2007-03-20, Last modification date: 2023-10-25)

Primary citation

Mizushima, T.,Yoshida, Y.,Kumanomidou, T.,Hasegawa, Y.,Suzuki, A.,Yamane, T.,Tanaka, K.
Structural basis for the selection of glycosylated substrates by SCFFbs1 ubiquitin ligase
Proc.Natl.Acad.Sci.Usa, 104:5777-5781, 2007

PubMed Abstract: 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.

PubMed: 17389369
DOI: 10.1073/pnas.0610312104

Experimental method

X-RAY DIFFRACTION (3.52 Å)