6HB1
Structure of Hgh1, crystal form I
Summary for 6HB1
| Entry DOI | 10.2210/pdb6hb1/pdb |
| Descriptor | Protein HGH1, CHLORIDE ION (3 entities in total) |
| Functional Keywords | solenoid protein, armadillo repeat, chaperone |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) |
| Total number of polymer chains | 4 |
| Total formula weight | 167672.08 |
| Authors | Moenkemeyer, L.,Klaips, C.L.,Balchin, D.,Koerner, R.,Hartl, F.U.,Bracher, A. (deposition date: 2018-08-09, release date: 2019-02-27, Last modification date: 2024-01-17) |
| Primary citation | Monkemeyer, L.,Klaips, C.L.,Balchin, D.,Korner, R.,Hartl, F.U.,Bracher, A. Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2. Mol.Cell, 74:88-100.e9, 2019 Cited by PubMed Abstract: Eukaryotic elongation factor 2 (eEF2) is an abundant and essential component of the translation machinery. The biogenesis of this 93 kDa multi-domain protein is assisted by the chaperonin TRiC/CCT. Here, we show in yeast cells that the highly conserved protein Hgh1 (FAM203 in humans) is a chaperone that cooperates with TRiC in eEF2 folding. In the absence of Hgh1, a substantial fraction of newly synthesized eEF2 is degraded or aggregates. We solved the crystal structure of Hgh1 and analyzed the interaction of wild-type and mutant Hgh1 with eEF2. These experiments revealed that Hgh1 is an armadillo repeat protein that binds to the dynamic central domain III of eEF2 via a bipartite interface. Hgh1 binding recruits TRiC to the C-terminal eEF2 module and prevents unproductive interactions of domain III, allowing efficient folding of the N-terminal GTPase module. eEF2 folding is completed upon dissociation of TRiC and Hgh1. PubMed: 30876804DOI: 10.1016/j.molcel.2019.01.034 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.33 Å) |
Structure validation
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