The crystal structure of protein-transporting chaperone BCP1 from Saccharomyces cerevisiae
Journal
Journal of Structural Biology
Journal Volume
212
Journal Volume
212
Journal Issue
1
Journal Issue
1
ISSN
10478477
Date Issued
2020-10-01
Author(s)
Abstract
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.
Subjects
BCP1
Chaperone
Crystal structure
GNAT
PF13862
SDGs
Publisher
Academic Press Inc.
Description
Article number: 107605
Type
journal article