5MZU
Crystal structure of the myosin chaperone UNC-45 from C. elegans (alternative conformation)
Summary for 5MZU
| Entry DOI | 10.2210/pdb5mzu/pdb |
| Related | 4I2Z |
| Descriptor | UNC-45 (1 entity in total) |
| Functional Keywords | chaperone, myosin folding, protein filament, ucs domain, arm repeats |
| Biological source | Caenorhabditis elegans |
| Total number of polymer chains | 1 |
| Total formula weight | 108552.90 |
| Authors | Hellerschmied, D.,Gazda, L.,Clausen, T. (deposition date: 2017-02-01, release date: 2018-02-14, Last modification date: 2024-11-13) |
| Primary citation | Hellerschmied, D.,Roessler, M.,Lehner, A.,Gazda, L.,Stejskal, K.,Imre, R.,Mechtler, K.,Dammermann, A.,Clausen, T. UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins. Nat Commun, 9:484-484, 2018 Cited by PubMed Abstract: Muscle development requires the coordinated activities of specific protein folding and degradation factors. UFD-2, a U-box ubiquitin ligase, has been reported to play a central role in this orchestra regulating the myosin chaperone UNC-45. Here, we apply an integrative in vitro and in vivo approach to delineate the substrate-targeting mechanism of UFD-2 and elucidate its distinct mechanistic features as an E3/E4 enzyme. Using Caenorhabditis elegans as model system, we demonstrate that UFD-2 is not regulating the protein levels of UNC-45 in muscle cells, but rather shows the characteristic properties of a bona fide E3 ligase involved in protein quality control. Our data demonstrate that UFD-2 preferentially targets unfolded protein segments. Moreover, the UNC-45 chaperone can serve as an adaptor protein of UFD-2 to poly-ubiquitinate unfolded myosin, pointing to a possible role of the UFD-2/UNC-45 pair in maintaining proteostasis in muscle cells. PubMed: 29396393DOI: 10.1038/s41467-018-02924-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.8 Å) |
Structure validation
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