5YCA

Crystal structure of inner membrane protein Bqt4 in complex with LEM2

5YCA の概要

• エントリーDOI: 10.2210/pdb5yca/pdb
• 分子名称: Ubiquitin-like protein SMT3,Bouquet formation protein 4, Lap-Emerin-Man domain protein 2 (3 entities in total)
• 機能のキーワード: chromosome organization, membrane organization, bouquet formation, lap-emerin-man domain protein, membrane protein
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25943.36

構造登録者

Chen, Y.,Hu, C. (登録日: 2017-09-07, 公開日: 2018-11-14, 最終更新日: 2023-11-22)

主引用文献

Hu, C.,Inoue, H.,Sun, W.,Takeshita, Y.,Huang, Y.,Xu, Y.,Kanoh, J.,Chen, Y.
Structural insights into chromosome attachment to the nuclear envelope by an inner nuclear membrane protein Bqt4 in fission yeast.
Nucleic Acids Res., 47:1573-1584, 2019

PubMed Abstract: The dynamic association of chromosomes with the nuclear envelope (NE) is essential for chromosome maintenance. Schizosaccharomyces pombe inner nuclear membrane protein Bqt4 plays a critical role in connecting telomeres to the NE, mainly through a direct interaction with the telomeric protein Rap1. Bqt4 also interacts with Lem2 for pericentric heterochromatin maintenance. How Bqt4 coordinates the interactions with different proteins to exert their functions is unclear. Here, we report the crystal structures of the N-terminal domain of Bqt4 in complexes with Bqt4-binding motifs from Rap1, Lem2, and Sad1. The structural, biochemical and cellular analyses reveal that the N-terminal domain of Bqt4 is a protein-interaction module that recognizes a consensus motif and plays essential roles in telomere-NE association and meiosis progression. Phosphorylation of Bqt4-interacting proteins may act as a switch to regulate these interactions during cell cycles. Our studies provide structural insights into the identification and regulation of Bqt4-mediated interactions.

PubMed: 30462301
DOI: 10.1093/nar/gky1186

実験手法

X-RAY DIFFRACTION (1.57 Å)