3AXC

Crystal structure of linear diubiquitin

Summary for 3AXC

• Entry DOI: 10.2210/pdb3axc/pdb
• Descriptor: Ubiquitin, GLYCEROL (3 entities in total)
• Functional Keywords: nf kappa b signaling, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Ubiquitin: Cytoplasm : P62979
• Total number of polymer chains: 1
• Total formula weight: 17371.88

Authors

Rohaim, A.,Kawasaki, M.,Kato, R.,Dikic, I.,Wakatsuki, S. (deposition date: 2011-04-01, release date: 2012-01-25, Last modification date: 2023-11-01)

Primary citation

Rohaim, A.,Kawasaki, M.,Kato, R.,Dikic, I.,Wakatsuki, S.
Structure of a compact conformation of linear diubiquitin
Acta Crystallogr.,Sect.D, 68:102-108, 2012

PubMed Abstract: Post-translational modifications involving ubiquitin regulate a wide range of biological processes including protein degradation, responses to DNA damage and immune signalling. Ubiquitin polymerizes into chains which may contain eight different linkage types; the ubiquitin C-terminal glycine can link to one of the seven lysine residues or the N-terminal amino group of methionine in the distal ubiquitin molecule. The latter head-to-tail linkage type, referred to as a linear ubiquitin chain, is involved in NF-κB activation through specific interactions with NF-κB essential modulator (NEMO). Here, a crystal structure of linear diubiquitin at a resolution of 2.2 Å is reported. Although the two ubiquitin moieties do not interact with each other directly, the overall structure adopts a compact but not completely closed conformation with a few intermoiety contacts. This structure differs from the previously reported extended conformation, which resembles Lys63-linked diubiquitin, suggesting that the linear polyubiquitin chain is intrinsically flexible and can adopt multiple conformations.

PubMed: 22281738
DOI: 10.1107/S0907444911051195

Experimental method

X-RAY DIFFRACTION (2.19 Å)