4GMQ

Ribosome-binding domain of Zuo1

Summary for 4GMQ

• Entry DOI: 10.2210/pdb4gmq/pdb
• Descriptor: Putative ribosome associated protein (2 entities in total)
• Functional Keywords: ribosome binding, co-translational chaperone, ribosome-binding protein
• Biological source: Chaetomium thermophilum var. thermophilum DSM 1495
• Total number of polymer chains: 1
• Total formula weight: 11064.67

Authors

Kopp, J.,Bange, G.,Sinning, I. (deposition date: 2012-08-16, release date: 2012-12-05, Last modification date: 2024-02-28)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.3 Å)