2MYX: Structure of the CUE domain of yeast Cue1

Ubiquitin conjugation is an essential process modulating protein function in eukaryotic cells. Surprisingly, little is known about how the progressive assembly of ubiquitin chains is managed by the responsible enzymes. Only recently has ubiquitin binding activity emerged as an important factor in chain formation. The Ubc7 activator Cue1 carries a ubiquitin binding CUE domain that substantially stimulates K48-linked polyubiquitination mediated by Ubc7. Our results from NMR-based analysis and in vitro ubiquitination reactions point out that two parameters accelerate ubiquitin chain assembly: the increasing number of CUE binding sites and the position of CUE binding within a growing chain. In particular, interactions with a ubiquitin moiety adjacent to the acceptor ubiquitin facilitate chain elongation. These data indicate a mechanism for ubiquitin binding in which Cue1 positions Ubc7 and the distal acceptor ubiquitin for rapid polyubiquitination. Disrupting this mechanism results in dysfunction of the ERAD pathway by a delayed turnover of substrates.
PDB ID: 2MYXDownload
MMDB ID: 137586
PDB Deposition Date: 2015/2/2
Updated in MMDB: 2016/08
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2MYX: monomeric; determined by author
Molecular Components in 2MYX
Label Count Molecule
Protein (1 molecule)
Coupling of Ubiquitin Conjugation to ER Degradation Protein 1(Gene symbol: CUE1)
Molecule annotation
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Citing MMDB