7C4H

Crystal structure of BCP1 from Saccharomyces Cerevisiae

7C4H の概要

• エントリーDOI: 10.2210/pdb7c4h/pdb
• 分子名称: Protein BCP1, CALCIUM ION (3 entities in total)
• 機能のキーワード: ribosome biosynthesis, chaperone
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67591.10

構造登録者

Chang, W.C.,Lin, M.H.,Hsu, C.H. (登録日: 2020-05-17, 公開日: 2020-12-09, 最終更新日: 2024-03-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.83 Å)