4HS2

Crystal Structure of the Human SPOP C-terminal Domain

4HS2 の概要

• エントリーDOI: 10.2210/pdb4hs2/pdb
• 分子名称: Speckle-type POZ protein (2 entities in total)
• 機能のキーワード: protein interaction domain, oligomerisation, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: O43791
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11941.45

構造登録者

Van Geersdaele, L.K.,Stead, M.A.,Carr, S.B.,Wright, S.C. (登録日: 2012-10-29, 公開日: 2013-09-11, 最終更新日: 2024-02-28)

主引用文献

van Geersdaele, L.K.,Stead, M.A.,Harrison, C.M.,Carr, S.B.,Close, H.J.,Rosbrook, G.O.,Connell, S.D.,Wright, S.C.
Structural basis of high-order oligomerization of the cullin-3 adaptor SPOP.
Acta Crystallogr.,Sect.D, 69:1677-1684, 2013

PubMed Abstract: Protein ubiquitination in eukaryotic cells is mediated by diverse E3 ligase enzymes that each target specific substrates. The cullin E3 ligase complexes are the most abundant class of E3 ligases; they contain various cullin components that serve as scaffolds for interaction with substrate-recruiting adaptor proteins. SPOP is a BTB-domain adaptor of the cullin-3 E3 ligase complexes; it selectively recruits substrates via its N-terminal MATH domain, whereas its BTB domain mediates dimerization and interactions with cullin-3. It has recently been recognized that the high-order oligomerization of SPOP enhances the ubiquitination of substrates. Here, a dimerization interface in the SPOP C-terminus is identified and it is shown that the dimerization interfaces of the BTB domain and of the C-terminus act independently and in tandem to generate high-order SPOP oligomers. The crystal structure of the dimeric SPOP C-terminal domain is reported at 1.5 Å resolution and it is shown that Tyr353 plays a critical role in high-order oligomerization. A model of the high-order SPOP oligomer is presented that depicts a helical organization that could enhance the efficiency of substrate ubiquitination.

PubMed: 23999291
DOI: 10.1107/S0907444913012687

実験手法

X-RAY DIFFRACTION (1.53 Å)