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4Y1H

Crystal structure of K33 linked tri-Ubiquitin

Summary for 4Y1H
Entry DOI10.2210/pdb4y1h/pdb
DescriptorUbiquitin-40S ribosomal protein S27a, 1,2-ETHANEDIOL (3 entities in total)
Functional Keywordsk33, k33 linked tri-ubiquitin, signaling protein
Biological sourceBos taurus (cattle)
Total number of polymer chains1
Total formula weight8825.10
Authors
Kristariyanto, Y.A.,Abdul Rehman, S.A.,Choi, S.Y.,Ritorto, S.,Campbell, D.G.,Morrice, N.A.,Toth, R.,Kulathu, Y. (deposition date: 2015-02-07, release date: 2015-03-18, Last modification date: 2024-01-10)
Primary citationKristariyanto, Y.A.,Choi, S.Y.,Rehman, S.A.,Ritorto, M.S.,Campbell, D.G.,Morrice, N.A.,Toth, R.,Kulathu, Y.
Assembly and structure of Lys33-linked polyubiquitin reveals distinct conformations.
Biochem.J., 467:345-352, 2015
Cited by
PubMed Abstract: Ubiquitylation regulates a multitude of biological processes and this versatility stems from the ability of ubiquitin (Ub) to form topologically different polymers of eight different linkage types. Whereas some linkages have been studied in detail, other linkage types including Lys33-linked polyUb are poorly understood. In the present study, we identify an enzymatic system for the large-scale assembly of Lys33 chains by combining the HECT (homologous to the E6-AP C-terminus) E3 ligase AREL1 (apoptosis-resistant E3 Ub protein ligase 1) with linkage selective deubiquitinases (DUBs). Moreover, this first characterization of the chain selectivity of AREL1 indicates its preference for assembling Lys33- and Lys11-linked Ub chains. Intriguingly, the crystal structure of Lys33-linked diUb reveals that it adopts a compact conformation very similar to that observed for Lys11-linked diUb. In contrast, crystallographic analysis of Lys33-linked triUb reveals a more extended conformation. These two distinct conformational states of Lys33-linked polyUb may be selectively recognized by Ub-binding domains (UBD) and enzymes of the Ub system. Importantly, our work provides a method to assemble Lys33-linked polyUb that will allow further characterization of this atypical chain type.
PubMed: 25723849
DOI: 10.1042/BJ20141502
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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