4GNI

Structure of the Ssz1 ATPase bound to ATP and Magnesium

4GNI の概要

• エントリーDOI: 10.2210/pdb4gni/pdb
• 関連するPDBエントリー: 4GMQ
• 分子名称: Putative heat shock protein, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: hsp70-type atpase, atp binding protein, magnesium binding, co-translational chaperone, ribosome-associated complex, rac, chaperone
• 由来する生物種: Chaetomium thermophilum var. thermophilum DSM 1495
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89968.35

構造登録者

Bange, G.,Sinning, I. (登録日: 2012-08-17, 公開日: 2012-12-05, 最終更新日: 2024-02-28)

主引用文献

Leidig, C.,Bange, G.,Kopp, J.,Amlacher, S.,Aravind, A.,Wickles, S.,Witte, G.,Hurt, E.,Beckmann, R.,Sinning, I.
Structural characterization of a eukaryotic chaperone-the ribosome-associated complex.
Nat.Struct.Mol.Biol., 20:23-28, 2013

PubMed Abstract: Ribosome-associated chaperones act in early folding events during protein synthesis. Structural information is available for prokaryotic chaperones (such as trigger factor), but structural understanding of these processes in eukaryotes lags far behind. Here we present structural analyses of the eukaryotic ribosome-associated complex (RAC) from Saccharomyces cerevisiae and Chaetomium thermophilum, consisting of heat-shock protein 70 (Hsp70) Ssz1 and the Hsp40 Zuo1. RAC is an elongated complex that crouches over the ribosomal tunnel exit and seems to be stabilized in a distinct conformation by expansion segment ES27. A unique α-helical domain in Zuo1 mediates ribosome interaction of RAC near the ribosomal proteins L22e and L31e and ribosomal RNA helix H59. The crystal structure of the Ssz1 ATPase domain bound to ATP-Mg²⁺ explains its catalytic inactivity and suggests that Ssz1 may act before the RAC-associated chaperone Ssb. Our study offers insights into the interplay between RAC, the ER membrane-integrated Hsp40-type protein ERj1 and the signal-recognition particle.

PubMed: 23202586
DOI: 10.1038/nsmb.2447

実験手法

X-RAY DIFFRACTION (1.796 Å)