2LVP
gp78CUE domain bound to the distal ubiquitin of K48-linked diubiquitin
Summary for 2LVP
Entry DOI | 10.2210/pdb2lvp/pdb |
Related | 2LVN 2LVO 2LVQ |
NMR Information | BMRB: 18583 |
Descriptor | Ubiquitin, E3 ubiquitin-protein ligase AMFR (2 entities in total) |
Functional Keywords | cue domain, signaling protein-ligase complex, signaling protein/ligase |
Biological source | Homo sapiens (human) More |
Cellular location | Ubiquitin: Cytoplasm (By similarity): P0CG48 Endoplasmic reticulum membrane; Multi-pass membrane protein: Q9UKV5 |
Total number of polymer chains | 3 |
Total formula weight | 23120.41 |
Authors | Liu, S.,Chen, Y.,Huang, T.,Tarasov, S.G.,King, A.,Li, J.,Weissman, A.M.,Byrd, R.A.,Das, R. (deposition date: 2012-07-09, release date: 2012-11-21, Last modification date: 2024-05-15) |
Primary citation | Liu, S.,Chen, Y.,Li, J.,Huang, T.,Tarasov, S.,King, A.,Weissman, A.M.,Byrd, R.A.,Das, R. Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains. Structure, 20:2138-2150, 2012 Cited by PubMed Abstract: Recognition of ubiquitin and polyubiquitin chains by ubiquitin-binding domains (UBDs) is vital for ubiquitin-mediated signaling pathways. The endoplasmic reticulum resident RING finger ubiquitin ligase (E3) gp78 regulates critical proteins via the ubiquitin-proteasome system to maintain cellular homeostasis and includes a UBD known as the CUE domain, which is essential for function. A probable role of this domain is to recognize ubiquitin-modified substrates, enabling gp78 to assemble polyubiquitin chains on these substrates and mark them for degradation. Here, we report the molecular details of the interaction of gp78CUE domain with ubiquitin and diubiquitin. The gp78CUE domain exhibits a well-defined set of interactions with ubiquitin and a dynamic, promiscuous interaction with diubiquitin chains. This leads to a model in which the CUE domain functions to both facilitate substrate binding and enable switching between adjacent ubiquitin molecules of a growing chain to enable processivity in ubiquitination. PubMed: 23123110DOI: 10.1016/j.str.2012.09.020 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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