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4BOZ

Structure of OTUD2 OTU domain in complex with K11-linked di ubiquitin

Summary for 4BOZ
Entry DOI10.2210/pdb4boz/pdb
Related4BOP 4BOQ 4BOS 4BOU
DescriptorUBIQUITIN THIOESTERASE OTU1, UBIQUITIN-C, GLYCEROL, ... (4 entities in total)
Functional Keywordshydrolase
Biological sourceHOMO SAPIENS (HUMAN)
More
Cellular locationUbiquitin: Cytoplasm (By similarity): P0CG48
Total number of polymer chains5
Total formula weight67315.22
Authors
Primary citationMevissen, T.E.T.,Hospenthal, M.K.,Geurink, P.P.,Elliott, P.R.,Akutsu, M.,Arnaudo, N.,Ekkebus, R.,Kulathu, Y.,Wauer, T.,El Oualid, F.,Freund, S.M.V.,Ovaa, H.,Komander, D.
Otu Deubiquitinases Reveal Mechanisms of Linkage Specificity and Enable Ubiquitin Chain Restriction Analysis.
Cell(Cambridge,Mass.), 154:169-, 2013
Cited by
PubMed Abstract: Sixteen ovarian tumor (OTU) family deubiquitinases (DUBs) exist in humans, and most members regulate cell-signaling cascades. Several OTU DUBs were reported to be ubiquitin (Ub) chain linkage specific, but comprehensive analyses are missing, and the underlying mechanisms of linkage specificity are unclear. Using Ub chains of all eight linkage types, we reveal that most human OTU enzymes are linkage specific, preferring one, two, or a defined subset of linkage types, including unstudied atypical Ub chains. Biochemical analysis and five crystal structures of OTU DUBs with or without Ub substrates reveal four mechanisms of linkage specificity. Additional Ub-binding domains, the ubiquitinated sequence in the substrate, and defined S1' and S2 Ub-binding sites on the OTU domain enable OTU DUBs to distinguish linkage types. We introduce Ub chain restriction analysis, in which OTU DUBs are used as restriction enzymes to reveal linkage type and the relative abundance of Ub chains on substrates.
PubMed: 23827681
DOI: 10.1016/J.CELL.2013.05.046
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.03 Å)
Structure validation

227111

數據於2024-11-06公開中

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