Acta crystallographica. Section F, Structural biology communications, 2016-08, Vol.72 (8), p.619-626
2016
Details
- Autor(en) / Beteiligte
- Titel
- Structural analysis of a function-associated loop mutant of the substrate-recognition domain of Fbs1 ubiquitin ligase
- Ist Teil von
- Acta crystallographica. Section F, Structural biology communications, 2016-08, Vol.72 (8), p.619-626
- Ort / Verlag
- 5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography
- Erscheinungsjahr
- 2016
- Link zum Volltext
- Quelle
- Wiley-Blackwell Full Collection
- Beschreibungen/Notizen
- 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. The crystal structure of the substrate‐recognition domain of an Fbs1 mutant was determined at a resolution of 2.3 Å. Comparison of the wild‐type and mutant Fbs1 structures provides insight into the structural features of this carbohydrate‐binding site.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 2053-230XeISSN: 2053-230XDOI: 10.1107/S2053230X16011018Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4973303
- Format
- –
- Schlagworte
- Amino Acid Sequence, Binding Sites, Cell Cycle Proteins - chemistry, Cell Cycle Proteins - genetics, Cell Cycle Proteins - metabolism, Cloning, Molecular, Crystallography, X-Ray, Escherichia coli - genetics, Escherichia coli - metabolism, F-box protein, F-Box Proteins - chemistry, F-Box Proteins - genetics, F-Box Proteins - metabolism, Fbs1, Gene Expression, glycoproteins, Humans, Hydrogen Bonding, Models, Molecular, Mutation, Nerve Tissue Proteins - chemistry, Nerve Tissue Proteins - genetics, Nerve Tissue Proteins - metabolism, Plasmids - chemistry, Plasmids - metabolism, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Recombinant Proteins - chemistry, Recombinant Proteins - genetics, Recombinant Proteins - metabolism, Research Communications, SCF E3 ubiquitin ligase, Sequence Alignment, Sequence Homology, Amino Acid, sequence-structure relationship, SKP Cullin F-Box Protein Ligases - chemistry, SKP Cullin F-Box Protein Ligases - genetics, SKP Cullin F-Box Protein Ligases - metabolism, Structure-Activity Relationship, Substrate Specificity