6hfo | pdb_00006hfo

Human Hsp90 co-chaperone TTC4 C-domain

spinqualitylabelsall models 6hfo, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hfo is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Related: 6hfm Gene: TTC4, My044 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The Hsp90 chaperone machinery in eukaryotes comprises a number of distinct accessory factors. Cns1 is one of the few essential co-chaperones in yeast, but its structure and function remained unknown. Here, we report the X-ray structure of the Cns1 fold and NMR studies on the partly disordered, essential segment of the protein. We demonstrate that Cns1 is important for maintaining translation elongation, specifically chaperoning the elongation factor eEF2. In this context, Cns1 interacts with the novel co-factor Hgh1 and forms a quaternary complex together with eEF2 and Hsp90. The in vivo folding and solubility of eEF2 depend on the presence of these proteins. Chaperoning of eEF2 by Cns1 is essential for yeast viability and requires a defined subset of the Hsp90 machinery as well as the identified eEF2 recruiting factor Hgh1. The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2.,Schopf FH, Huber EM, Dodt C, Lopez A, Biebl MM, Rutz DA, Muhlhofer M, Richter G, Madl T, Sattler M, Groll M, Buchner J Mol Cell. 2019 Mar 8. pii: S1097-2765(19)30101-7. doi:, 10.1016/j.molcel.2019.02.011. PMID:30876805 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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