5K9P

Ser20 phosphorylated ubiquitin

Summary for 5K9P

• Entry DOI: 10.2210/pdb5k9p/pdb
• Descriptor: Polyubiquitin-B (2 entities in total)
• Functional Keywords: ubiquitin, phosphoubiquitin, phospho-ubiquitin, cell cycle, signaling protein
• Biological source: Homo sapiens (Human)
• Cellular location: Ubiquitin: Cytoplasm : P0CG47
• Total number of polymer chains: 1
• Total formula weight: 8656.81

Authors

Huguenin-Dezot, N.,Chin, J.W. (deposition date: 2016-06-01, release date: 2016-07-20, Last modification date: 2024-11-06)

Primary citation

Huguenin-Dezot, N.,De Cesare, V.,Peltier, J.,Knebel, A.,Kristaryianto, Y.A.,Rogerson, D.T.,Kulathu, Y.,Trost, M.,Chin, J.W.
Synthesis of Isomeric Phosphoubiquitin Chains Reveals that Phosphorylation Controls Deubiquitinase Activity and Specificity.
Cell Rep, 16:1180-1193, 2016

PubMed Abstract: Ubiquitin is post-translationally modified by phosphorylation at several sites, but the consequences of these modifications are largely unknown. Here, we synthesize multi-milligram quantities of ubiquitin phosphorylated at serine 20, serine 57, and serine 65 via genetic code expansion. We use these phosphoubiquitins for the enzymatic assembly of 20 isomeric phosphoubiquitin dimers, with different sites of isopeptide linkage and/or phosphorylation. We discover that phosphorylation of serine 20 on ubiquitin converts UBE3C from a dual-specificity E3 ligase into a ligase that primarily synthesizes K48 chains. We profile the activity of 31 deubiquitinases on the isomeric phosphoubiquitin dimers in 837 reactions, and we discover that phosphorylation at distinct sites in ubiquitin can activate or repress cleavage of a particular linkage by deubiquitinases and that phosphorylation at a single site in ubiquitin can control the specificity of deubiquitinases for distinct ubiquitin linkages.

PubMed: 27425610
DOI: 10.1016/j.celrep.2016.06.064

Experimental method

X-RAY DIFFRACTION (1.55 Å)