The crystal structure of protein-transporting chaperone BCP1 from Saccharomyces cerevisiae.
Binding Sites
/ physiology
Crystallography, X-Ray
/ methods
Nuclear Proteins
/ chemistry
Protein Conformation, beta-Strand
/ physiology
Protein Structure, Secondary
/ physiology
Ribosomal Proteins
/ chemistry
Ribosomes
/ metabolism
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ chemistry
BCP1
Chaperone
Crystal structure
GNAT
PF13862
Journal
Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206
Informations de publication
Date de publication:
01 10 2020
01 10 2020
Historique:
received:
26
05
2020
revised:
04
08
2020
accepted:
12
08
2020
pubmed:
18
8
2020
medline:
14
10
2021
entrez:
18
8
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32805410
pii: S1047-8477(20)30178-7
doi: 10.1016/j.jsb.2020.107605
pii:
doi:
Substances chimiques
Bcp1 protein, S cerevisiae
0
Nuclear Proteins
0
Ribosomal Proteins
0
Saccharomyces cerevisiae Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
107605Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.