6HB1

Structure of Hgh1, crystal form I

6HB1 の概要

• エントリーDOI: 10.2210/pdb6hb1/pdb
• 分子名称: Protein HGH1, CHLORIDE ION (3 entities in total)
• 機能のキーワード: solenoid protein, armadillo repeat, chaperone
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 167672.08

構造登録者

Moenkemeyer, L.,Klaips, C.L.,Balchin, D.,Koerner, R.,Hartl, F.U.,Bracher, A. (登録日: 2018-08-09, 公開日: 2019-02-27, 最終更新日: 2024-01-17)

主引用文献

Monkemeyer, L.,Klaips, C.L.,Balchin, D.,Korner, R.,Hartl, F.U.,Bracher, A.
Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2.
Mol.Cell, 74:88-100.e9, 2019

PubMed Abstract: Eukaryotic elongation factor 2 (eEF2) is an abundant and essential component of the translation machinery. The biogenesis of this 93 kDa multi-domain protein is assisted by the chaperonin TRiC/CCT. Here, we show in yeast cells that the highly conserved protein Hgh1 (FAM203 in humans) is a chaperone that cooperates with TRiC in eEF2 folding. In the absence of Hgh1, a substantial fraction of newly synthesized eEF2 is degraded or aggregates. We solved the crystal structure of Hgh1 and analyzed the interaction of wild-type and mutant Hgh1 with eEF2. These experiments revealed that Hgh1 is an armadillo repeat protein that binds to the dynamic central domain III of eEF2 via a bipartite interface. Hgh1 binding recruits TRiC to the C-terminal eEF2 module and prevents unproductive interactions of domain III, allowing efficient folding of the N-terminal GTPase module. eEF2 folding is completed upon dissociation of TRiC and Hgh1.

PubMed: 30876804
DOI: 10.1016/j.molcel.2019.01.034

実験手法

X-RAY DIFFRACTION (2.33 Å)