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5UJN

Representative 2-conformer ensembles of K27-linked Ub2 from RDC data

Summary for 5UJN
Entry DOI10.2210/pdb5ujn/pdb
Related5UJL
NMR InformationBMRB: 30234
DescriptorUbiquitin (1 entity in total)
Functional Keywordsdiubiquitin, k27, polyubiquitin chain, signaling protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight17153.66
Authors
Castaneda, C.A.,Fushman, D. (deposition date: 2017-01-18, release date: 2018-08-08, Last modification date: 2024-10-30)
Primary citationCastaneda, 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: 26876099
DOI: 10.1016/j.str.2016.01.007
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

238582

数据于2025-07-09公开中

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