4gmq | pdb_00004gmq

Ribosome-binding domain of Zuo1

spinqualitylabelsall models 4gmq, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gmq is a 1 chain structure with sequence from Chatd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: CTHT_0006310, Zuo1 (CHATD) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 alpha-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. Structural characterization of a eukaryotic chaperone-the ribosome-associated complex.,Leidig C, Bange G, Kopp J, Amlacher S, Aravind A, Wickles S, Witte G, Hurt E, Beckmann R, Sinning I Nat Struct Mol Biol. 2012 Dec 2. doi: 10.1038/nsmb.2447. PMID:23202586 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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