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.
Keywords:
F-box protein; Fbs1; SCF E3 ubiquitin ligase; glycoproteins; sequence–structure relationship.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Cell Cycle Proteins / chemistry*
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Cell Cycle Proteins / genetics
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Cell Cycle Proteins / metabolism
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Cloning, Molecular
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Crystallography, X-Ray
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Escherichia coli / genetics
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Escherichia coli / metabolism
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F-Box Proteins / chemistry*
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F-Box Proteins / genetics
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F-Box Proteins / metabolism
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Gene Expression
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Humans
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Hydrogen Bonding
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Models, Molecular
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Mutation
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Nerve Tissue Proteins / chemistry*
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism
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Plasmids / chemistry*
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Plasmids / metabolism
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Protein Binding
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Protein Conformation, alpha-Helical
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Protein Conformation, beta-Strand
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Protein Interaction Domains and Motifs
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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SKP Cullin F-Box Protein Ligases / chemistry*
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SKP Cullin F-Box Protein Ligases / genetics
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SKP Cullin F-Box Protein Ligases / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
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Structure-Activity Relationship
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Substrate Specificity
Substances
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Cell Cycle Proteins
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F-Box Proteins
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FBXO2 protein, human
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Nerve Tissue Proteins
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Recombinant Proteins
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SKP Cullin F-Box Protein Ligases