4Z9S

Non-covalent assembly of monoubiquitin that mimics K11 poly-ubiquitin

Summary for 4Z9S

• Entry DOI: 10.2210/pdb4z9s/pdb
• Descriptor: Ubiquitin-40S ribosomal protein S27a, MALONIC ACID, THIOCYANATE ION, ... (4 entities in total)
• Functional Keywords: cell cycle
• Biological source: Bos taurus (Bovine)
• Cellular location: Ubiquitin: Cytoplasm : P62992
• Total number of polymer chains: 4
• Total formula weight: 35454.43

Authors

Levin-Kravets, O.,Prag, G. (deposition date: 2015-04-11, release date: 2015-07-29, Last modification date: 2024-01-10)

Primary citation

Levin-Kravets, O.,Shohat, N.,Prag, G.
Tetrameric Assembly of Monoubiquitin Accurately Mimics the Lys11 Polyubiquitin Chain Structure.
Biochemistry, 54:4704-4710, 2015

PubMed Abstract: Specific lysine residues on the ubiquitin surface were selected during the course of evolution to form different polyubiquitin chain structures that signal diverse cellular processes. A vast number of ubiquitin receptors specifically recognize and decode the signals conferred by these polyubiquitin chains. The mechanisms of formation and the structure of Lys11-linked ubiquitin, which signals for cell-cycle and innate immune control, have been elucidated. Here, we present a new crystal structure of monomeric ubiquitin that accurately mimics one of the structures of Lys11-linked ubiquitin. Analysis of the ubiquitin:ubiquitin interface demonstrates structural fitness and specificity. The interaction is exclusively hydrophilic, leaving the Ile44 hydrophobic patch, a major recognition site for ubiquitin receptors, exposed. These noncovalent ubiquitin:ubiquitin interactions are nearly identical to those reported for Lys11-linked ubiquitin and seem to play a significant role in stabilizing the crystal structure without the isopeptide bond. In vitro cross-linking analysis with wild-type ubiquitin or its mutants partially mimics the interactions in the crystal. We suggest that these interactions may play a biological role in transmitting Lys11-linked ubiquitin chain-type cellular signals.

PubMed: 26171660
DOI: 10.1021/acs.biochem.5b00498

Experimental method

X-RAY DIFFRACTION (2.3 Å)