2RU6
The pure alternative state of ubiquitin
Summary for 2RU6
| Entry DOI | 10.2210/pdb2ru6/pdb |
| Related | 2RSU |
| NMR Information | BMRB: 11547 |
| Descriptor | Ubiquitin (1 entity in total) |
| Functional Keywords | ubiquitin, alternatively folded state, high-pressure nmr, q41n variant, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Ubiquitin: Cytoplasm (By similarity): P0CG48 |
| Total number of polymer chains | 1 |
| Total formula weight | 8562.81 |
| Authors | Kitazawa, S.,Kameda, T.,Kumo, A.,Utsumi, M.,Baxter, N.,Kato, K.,Williamson, M.P.,Kitahara, R. (deposition date: 2013-12-04, release date: 2014-02-12, Last modification date: 2024-05-15) |
| Primary citation | Kitazawa, S.,Kameda, T.,Kumo, A.,Yagi-Utsumi, M.,Baxter, N.J.,Kato, K.,Williamson, M.P.,Kitahara, R. Close Identity between Alternatively Folded State N2 of Ubiquitin and the Conformation of the Protein Bound to the Ubiquitin-Activating Enzyme Biochemistry, 53:447-449, 2014 Cited by PubMed Abstract: We present the nuclear Overhauser effect-based structure determination of the Q41N variant of ubiquitin at 2500 bar, where the alternatively folded N2 state is 97% populated. This allows us to characterize the structure of the "pure" N2 state of ubiquitin. The N2 state shows a substantial change in the orientation of strand β5 compared to that of the normal folded N1 state, which matches the changes seen upon binding of ubiquitin to ubiquitin-activating enzyme E1. The recognition of E1 by ubiquitin is therefore best explained by conformational selection rather than induced-fit motion. PubMed: 24401037DOI: 10.1021/bi401617n PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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