The crystal structure of protein-transporting chaperone BCP1 from Saccharomyces cerevisiae
| Autor: | Po-Chih Kuo, Meng-Hsuan Lin, Sheng-Chia Chen, Yu-Yung Chang, Chun-Hua Hsu, Yi-Chih Chiu |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Ribosomal Proteins
Saccharomyces cerevisiae Proteins Protein family Saccharomyces cerevisiae Antiparallel (biochemistry) Crystallography X-Ray Ribosome Protein Structure Secondary 03 medical and health sciences Structural Biology Ribosomal protein Nuclear export signal 030304 developmental biology 0303 health sciences Binding Sites biology Chemistry 030302 biochemistry & molecular biology Nuclear Proteins biology.organism_classification Biochemistry Docking (molecular) Chaperone (protein) biology.protein Protein Conformation beta-Strand Ribosomes |
| Zdroj: | Journal of structural biology. 212(1) |
| ISSN: | 1095-8657 |
| Popis: | BCP1 is a protein enriched in the nucleus that is required for Mss4 nuclear export and identified as the chaperone of ribosomal protein Rpl23 in Saccharomyces cerevisiae. According to sequence homology, BCP1 is related to the mammalian BRCA2-interacting protein BCCIP and belongs to the BCIP protein family (PF13862) in the Pfam database. However, the BCIP family has no discernible similarity to proteins with known structure. Here, we report the crystal structure of BCP1, presenting an α/β fold in which the central antiparallel β-sheet is flanked by helices. Protein structural classification revealed that BCP1 has similarity to the GNAT superfamily but no conserved substrate-binding residues. Further modeling and protein-protein docking work provide a plausible model to explain the interaction between BCP1 and Rpl23. Our structural analysis presents the first structure of BCIP family and provides a foundation for understanding the molecular basis of BCP1 as a chaperone of Rpl23 for ribosome biosynthesis. |
| Databáze: | OpenAIRE |
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