7C4H

Crystal structure of BCP1 from Saccharomyces Cerevisiae

Summary for 7C4H

• Entry DOI: 10.2210/pdb7c4h/pdb
• Descriptor: Protein BCP1, CALCIUM ION (3 entities in total)
• Functional Keywords: ribosome biosynthesis, chaperone
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 67591.10

Authors

Chang, W.C.,Lin, M.H.,Hsu, C.H. (deposition date: 2020-05-17, release date: 2020-12-09, Last modification date: 2024-03-27)

Primary citation

Lin, M.H.,Kuo, P.C.,Chiu, Y.C.,Chang, Y.Y.,Chen, S.C.,Hsu, C.H.
The crystal structure of protein-transporting chaperone BCP1 from Saccharomyces cerevisiae.
J.Struct.Biol., 212:107605-107605, 2020

PubMed 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.

PubMed: 32805410
DOI: 10.1016/j.jsb.2020.107605

Experimental method

X-RAY DIFFRACTION (1.83 Å)