5B4N

Structure analysis of function associated loop mutant of substrate recognition domain of Fbs1 ubiquitin ligase

Summary for 5B4N

• Entry DOI: 10.2210/pdb5b4n/pdb
• Descriptor: F-box only protein 2 (2 entities in total)
• Functional Keywords: scf e3 ubiquitin ligase, f-box protein, glycoproteins, sequence-structure relationship, ligase
• Biological source: Mus musculus (Mouse)
• Cellular location: Cytoplasm: Q80UW2
• Total number of polymer chains: 2
• Total formula weight: 47252.40

Authors

Nishio, K.,Yoshida, Y.,Tanaka, K.,Mizushima, T. (deposition date: 2016-04-06, release date: 2016-09-14, Last modification date: 2023-11-08)

Primary citation

Nishio, K.,Yoshida, Y.,Tanaka, K.,Mizushima, T.
Structural analysis of a function-associated loop mutant of the substrate-recognition domain of Fbs1 ubiquitin ligase
Acta Crystallogr.,Sect.F, 72:619-626, 2016

PubMed 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 (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.

PubMed: 27487926
DOI: 10.1107/S2053230X16011018

Experimental method

X-RAY DIFFRACTION (2.3 Å)