PDBsum entry 4gmq

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Ribosome-binding protein PDB id
Protein chain
92 a.a.
Waters ×182
PDB id:
Name: Ribosome-binding protein
Title: Ribosome-binding domain of zuo1
Structure: Putative ribosome associated protein. Chain: a. Fragment: unp residues 352-446. Engineered: yes
Source: Chaetomium thermophilum var. Thermophi 1495. Organism_taxid: 759272. Strain: dsm 1495 / cbs 144.50 / imi 039719. Gene: ctht_0006310, zuo1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
1.30Å     R-factor:   0.153     R-free:   0.188
Authors: J.Kopp,G.Bange,I.Sinning
Key ref: C.Leidig et al. (2013). Structural characterization of a eukaryotic chaperone--the ribosome-associated complex. Nat Struct Mol Biol, 20, 23-28. PubMed id: 23202586
16-Aug-12     Release date:   05-Dec-12    
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Protein chain
Pfam   ArchSchema ?
G0RYD6  (G0RYD6_CHATD) -  Putative ribosome associated protein
446 a.a.
92 a.a.
Key:    PfamA domain  Secondary structure  CATH domain


Nat Struct Mol Biol 20:23-28 (2013)
PubMed id: 23202586  
Structural characterization of a eukaryotic chaperone--the ribosome-associated complex.
C.Leidig, G.Bange, J.Kopp, S.Amlacher, A.Aravind, S.Wickles, G.Witte, E.Hurt, R.Beckmann, I.Sinning.
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-Mg(2+) 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.