4X86

Crystal structure of BAG6-Ubl4a complex

4X86 の概要

• エントリーDOI: 10.2210/pdb4x86/pdb
• 分子名称: Ubiquitin-like protein 4A, Large proline-rich protein BAG6, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE, ... (5 entities in total)
• 機能のキーワード: tail-anchored transmembrane protein biogenesis, quality control of proteins, protein binding
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16467.59

構造登録者

Kuwabara, N.,Kato, R. (登録日: 2014-12-10, 公開日: 2015-02-25, 最終更新日: 2024-03-20)

主引用文献

Kuwabara, N.,Minami, R.,Yokota, N.,Matsumoto, H.,Senda, T.,Kawahara, H.,Kato, R.
Structure of a BAG6 (Bcl-2-associated Athanogene 6)-Ubl4a (Ubiquitin-like Protein 4a) Complex Reveals a Novel Binding Interface That Functions in Tail-anchored Protein Biogenesis
J.Biol.Chem., 290:9387-9398, 2015

PubMed Abstract: BAG6 is an essential protein that functions in two distinct biological pathways, ubiquitin-mediated protein degradation of defective polypeptides and tail-anchored (TA) transmembrane protein biogenesis in mammals, although its structural and functional properties remain unknown. We solved a crystal structure of the C-terminal heterodimerization domains of BAG6 and Ubl4a and characterized their interaction biochemically. Unexpectedly, the specificity and structure of the C terminus of BAG6, which was previously classified as a BAG domain, were completely distinct from those of the canonical BAG domain. Furthermore, the tight association of BAG6 and Ubl4a resulted in modulation of Ubl4a protein stability in cells. Therefore, we propose to designate the Ubl4a-binding region of BAG6 as the novel BAG-similar (BAGS) domain. The structure of Ubl4a, which interacts with BAG6, is similar to the yeast homologue Get5, which forms a homodimer. These observations indicate that the BAGS domain of BAG6 promotes the TA protein biogenesis pathway in mammals by the interaction with Ubl4a.

PubMed: 25713138
DOI: 10.1074/jbc.M114.631804

実験手法

X-RAY DIFFRACTION (1.85 Å)