5UJN
Representative 2-conformer ensembles of K27-linked Ub2 from RDC data
Summary for 5UJN
Entry DOI | 10.2210/pdb5ujn/pdb |
Related | 5UJL |
NMR Information | BMRB: 30234 |
Descriptor | Ubiquitin (1 entity in total) |
Functional Keywords | diubiquitin, k27, polyubiquitin chain, signaling protein |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 17153.66 |
Authors | Castaneda, C.A.,Fushman, D. (deposition date: 2017-01-18, release date: 2018-08-08, Last modification date: 2024-10-30) |
Primary citation | Castaneda, C.A.,Dixon, E.K.,Walker, O.,Chaturvedi, A.,Nakasone, M.A.,Curtis, J.E.,Reed, M.R.,Krueger, S.,Cropp, T.A.,Fushman, D. Linkage via K27 Bestows Ubiquitin Chains with Unique Properties among Polyubiquitins. Structure, 24:423-436, 2016 Cited by PubMed Abstract: Polyubiquitination, a critical protein post-translational modification, signals for a diverse set of cellular events via the different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the ɛ-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. We assembled di-ubiquitins (Ub2) comprising every lysine linkage and examined them biochemically and structurally. Of these, K27-Ub2 is unique as it is not cleaved by most deubiquitinases. As this remains the only structurally uncharacterized lysine linkage, we comprehensively examined the structures and dynamics of K27-Ub2 using nuclear magnetic resonance, small-angle neutron scattering, and in silico ensemble modeling. Our structural data provide insights into the functional properties of K27-Ub2, in particular that K27-Ub2 may be specifically recognized by K48-selective receptor UBA2 domain from proteasomal shuttle protein hHR23a. Binding studies and mutagenesis confirmed this prediction, further highlighting structural/recognition versatility of polyubiquitins and the potential power of determining function from elucidation of conformational ensembles. PubMed: 26876099DOI: 10.1016/j.str.2016.01.007 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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