2JKI

Complex of Hsp90 N-terminal and Sgt1 CS domain

2JKI の概要

• エントリーDOI: 10.2210/pdb2jki/pdb
• 分子名称: CYTOSOLIC HEAT SHOCK PROTEIN 90, SGT1-LIKE PROTEIN, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: hsp90 sgt1, stress response, chaperone
• 由来する生物種: HORDEUM VULGARE (BARLEY); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 108088.60

構造登録者

Zhang, M.,Pearl, L.H. (登録日: 2008-08-28, 公開日: 2008-10-07, 最終更新日: 2023-12-13)

主引用文献

Zhang, M.,Boter, M.,Li, K.,Kadota, Y.,Panaretou, B.,Prodromou, C.,Shirasu, K.,Pearl, L.H.
Structural and Functional Coupling of Hsp90- and Sgt1-Centred Multi-Protein Complexes.
Embo J., 27:2789-, 2008

PubMed Abstract: Sgt1 is an adaptor protein implicated in a variety of processes, including formation of the kinetochore complex in yeast, and regulation of innate immunity systems in plants and animals. Sgt1 has been found to associate with SCF E3 ubiquitin ligases, the CBF3 kinetochore complex, plant R proteins and related animal Nod-like receptors, and with the Hsp90 molecular chaperone. We have determined the crystal structure of the core Hsp90-Sgt1 complex, revealing a distinct site of interaction on the Hsp90 N-terminal domain. Using the structure, we developed mutations in Sgt1 interfacial residues, which specifically abrogate interaction with Hsp90, and disrupt Sgt1-dependent functions in vivo, in plants and yeast. We show that Sgt1 bridges the Hsp90 molecular chaperone system to the substrate-specific arm of SCF ubiquitin ligase complexes, suggesting a role in SCF assembly and regulation, and providing multiple complementary routes for ubiquitination of Hsp90 client proteins.

PubMed: 18818696
DOI: 10.1038/EMBOJ.2008.190

実験手法

X-RAY DIFFRACTION (3.3 Å)