Crystal structure of yeast Gid10 in complex with Pro/N-degron
| Autor: | Jiwon Heo, Hyun Kyu Song, Leehyeon Kim, Jin Seok Shin, Si Hoon Park |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Protein Conformation alpha-Helical Saccharomyces cerevisiae Proteins Proline Ubiquitin-Protein Ligases Genetic Vectors Saccharomyces cerevisiae Vesicular Transport Proteins Biophysics GID complex Gene Expression Crystallography X-Ray Biochemistry Substrate Specificity Residue (chemistry) Escherichia coli Protein Interaction Domains and Motifs Amino Acid Sequence Cloning Molecular Molecular Biology chemistry.chemical_classification DNA ligase Binding Sites Sequence Homology Amino Acid biology Substrate (chemistry) Cell Biology biology.organism_classification Recombinant Proteins Yeast Ubiquitin ligase chemistry Proteolysis biology.protein Protein Conformation beta-Strand Degron Oligopeptides Sequence Alignment Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 582:86-92 |
| ISSN: | 0006-291X |
| Popis: | The cellular glucose level has to be tightly regulated by a variety of cellular processes. One of them is the degradation of gluconeogenic enzymes such as Fbp1, Icl1, Mdh2, and Pck1 by GID (glucose-induced degradation deficient) E3 ubiquitin ligase. The Gid4 component of the GID ligase complex is responsible for recognizing the N-terminal proline residue of the target substrates under normal conditions. However, an alternative N-recognin Gid10 controls the degradation process under stressed conditions. Although Gid10 shares a high sequence similarity with Gid4, their substrate specificities are quite different. Here, we report the structure of Gid10 from Saccharomyces cerevisiae in complex with Pro/N-degron, Pro-Tyr-Ile-Thr, which is almost identical to the sequence of the natural substrate Art2. Although Gid10 shares many structural features with the Gid4 protein from yeast and humans, the current structure explains the unique structural difference for the preference of bulky hydrophobic residue at the second position of Pro/N-degron. Therefore, this study provides a fundamental basis for understanding of the structural diversity and substrate specificity of recognition components in the GID E3 ligase complex involved in the Pro/N-degron pathway. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect