The crystal structure of protein-transporting chaperone BCP1 from Saccharomyces cerevisiae.

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.

journal_name

J Struct Biol

authors

Lin MH,Kuo PC,Chiu YC,Chang YY,Chen SC,Hsu CH

doi

10.1016/j.jsb.2020.107605

subject

Has Abstract

pub_date

2020-10-01 00:00:00

pages

107605

issue

1

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(20)30178-7

journal_volume

212

pub_type

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