5mb9

Crystal structure of the eukaryotic ribosome associated complex (RAC), a unique Hsp70/Hsp40 pair

spinqualitylabelsall models 5mb9, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mb9 is a 4 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: ATP, GOL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0RZX9_CHATD Publication Abstract from PubMed Cotranslational chaperones assist de novo folding of nascent polypeptides, prevent them from aggregating and modulate translation. The ribosome-associated complex (RAC) is unique in that the Hsp40 protein Zuo1 and the atypical Hsp70 chaperone Ssz1 form a stable heterodimer, which acts as a cochaperone for the Hsp70 chaperone Ssb. Here we present the structure of the Chaetomium thermophilum RAC core comprising Ssz1 and the Zuo1 N terminus. We show how the conserved allostery of Hsp70 proteins is abolished and this Hsp70-Hsp40 pair is molded into a functional unit. Zuo1 stabilizes Ssz1 in trans through interactions that in canonical Hsp70s occur in cis. Ssz1 is catalytically inert and cannot adopt the closed conformation, but the substrate binding domain beta is completed by Zuo1. Our study offers insights into the coupling of a special Hsp70-Hsp40 pair, which evolved to link protein folding and translation. Structural insights into a unique Hsp70-Hsp40 interaction in the eukaryotic ribosome-associated complex.,Weyer FA, Gumiero A, Gese GV, Lapouge K, Sinning I Nat Struct Mol Biol. 2017 Jan 9. doi: 10.1038/nsmb.3349. PMID:28067917 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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