Premium
Structural analysis of a function‐associated loop mutant of the substrate‐recognition domain of Fbs1 ubiquitin ligase
Author(s) -
Nishio Kazuya,
Yoshida Yukiko,
Tanaka Keiji,
Mizushima Tsunehiro
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16011018
Subject(s) - ubiquitin ligase , ubiquitin , mutant , dna ligase , loop (graph theory) , microbiology and biotechnology , function (biology) , chemistry , computational biology , substrate (aquarium) , domain (mathematical analysis) , biology , biophysics , biochemistry , enzyme , mathematics , gene , ecology , mathematical analysis , combinatorics
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 (β1, β2–β3, β3–β4, β5–β6, β7–β8 and β9–β10) 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.