Structural analysis of a function-associated loop mutant of the substrate-recognition domain of Fbs1 ubiquitin ligase

The SCF ubiquitin ligase comprises four components: Skp1, Cul1, Rbx1 and a variable-subunit F-box protein. The F-box protein Fbs1, which recognizes the N-linked glycoproteins, is involved in the endoplasmic reticulum-associated degradation pathway. Although FBG3, another F-box protein, shares 51% sequence identity with Fbs1, FBG3 does not bind glycoproteins. To investigate the sequence – structure relationship of the substrate-binding pocket, the crystal structure of a mutant substrate-binding domain of Fbs1 in which the six nonconserved regions ( β 1, β 2 – β 3, β 3 – β 4, β 5 – β 6, β 7 – β 8 and β 9 – β 10) of Fbs1 were substituted with those of FBG3 was determined. The substrate-binding pocket of this model exhibits structural features that differ from those of Fsb1.

Source: Acta Crystallographica Section F - July 26, 2016 Category: Biochemistry Authors: Nishio, K. Yoshida, Y. Tanaka, K. Mizushima, T. Tags: SCF E3 ubiquitin ligase F-box protein glycoproteins sequence – structure relationship Fbs1 research communications Source Type: research