Unknown

Dataset Information

0

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


ABSTRACT: 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 (?1, ?2-?3, ?3-?4, ?5-?6, ?7-?8 and ?9-?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.

SUBMITTER: Nishio K 

PROVIDER: S-EPMC4973303 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Nishio Kazuya K   Yoshida Yukiko Y   Tanaka Keiji K   Mizushima Tsunehiro T  

Acta crystallographica. Section F, Structural biology communications 20160727 Pt 8


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 dom  ...[more]

Similar Datasets

| S-EPMC6557900 | biostudies-literature
| S-EPMC1851568 | biostudies-literature
| S-EPMC2797283 | biostudies-literature
| S-EPMC10873202 | biostudies-literature
| S-EPMC5970261 | biostudies-literature
| S-EPMC10802466 | biostudies-literature
2020-08-15 | GSE148458 | GEO
| S-EPMC4031523 | biostudies-literature
| S-EPMC4445864 | biostudies-literature
2024-02-12 | PXD045837 | Pride