2MI8
Solution structure of lysine-free (K0) ubiquitin
Summary for 2MI8
Entry DOI | 10.2210/pdb2mi8/pdb |
NMR Information | BMRB: 19670 |
Descriptor | Ubiquitin (1 entity in total) |
Functional Keywords | signaling protein |
Biological source | Homo sapiens (human) |
Cellular location | Ubiquitin: Cytoplasm (By similarity): P0CG48 |
Total number of polymer chains | 1 |
Total formula weight | 8772.93 |
Authors | Huang, T.,Li, J.R.,Byrd, A.R. (deposition date: 2013-12-09, release date: 2014-04-02, Last modification date: 2024-05-15) |
Primary citation | Huang, T.,Li, J.,Byrd, R.A. Solution structure of lysine-free (K0) ubiquitin. Protein Sci., 23:662-667, 2014 Cited by PubMed Abstract: Lysine-free ubiquitin (K0-Ub) is commonly used to study the ubiquitin-signaling pathway, where it is assumed to have the same structure and function as wild-type ubiquitin (wt-Ub). However, the K0-Ub (15) N heteronuclear single quantum correlation NMR spectrum differs significantly from wt-Ub and the melting temperature is depressed by 19°C, raising the question of the structural integrity and equivalence to wt-Ub. The three-dimensional structure of K0-Ub was determined by solution NMR, using chemical shift and residual dipolar coupling data. K0-Ub adopts the same backbone structure as wt-Ub, and all significant chemical shifts can be related to interactions impacted by the K to R mutations. PubMed: 24591328DOI: 10.1002/pro.2450 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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