3ONS
Crystal structure of Human Ubiquitin in a new crystal form
Summary for 3ONS
| Entry DOI | 10.2210/pdb3ons/pdb |
| Descriptor | Ubiquitin (2 entities in total) |
| Functional Keywords | ubiquitin fold, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Ubiquitin: Cytoplasm (By similarity): P0CG47 |
| Total number of polymer chains | 1 |
| Total formula weight | 8192.38 |
| Authors | Amodeo, G.A.,Huang, K.Y.,Mcdermott, A.E.,Tong, L. (deposition date: 2010-08-30, release date: 2011-02-23, Last modification date: 2024-02-21) |
| Primary citation | Huang, K.Y.,Amodeo, G.A.,Tong, L.,McDermott, A. The structure of human ubiquitin in 2-methyl-2,4-pentanediol: a new conformational switch. Protein Sci., 20:630-639, 2011 Cited by PubMed Abstract: A new crystal structure of human ubiquitin is reported at 1.8 Å resolution. Compared with the other known crystal structure or the solution NMR structure of monomeric human ubiquitin, this new structure is similar in its overall fold but differs with respect to the conformation of the backbone in a surface-exposed region. The conformation reported here resembles conformations previously seen in complex with deubiquinating enzymes, wherein the Asp52/Gly53 main chain and Glu24 side chain move. This movement exposes the backbone carbonyl of Asp52 to the exterior of the molecule, making it possible to engage in hydrogen-bond contacts with neighboring molecules, rather than in an internal hydrogen bond with the backbone of Glu24. This particular crystal form of ubiquitin has been used in a large number of solid state NMR studies. The structure described here elucidates the origin of many of the chemical shift differences comparing solution and solid state studies. PubMed: 21432937DOI: 10.1002/pro.584 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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