2LVN

Structure of the gp78 CUE domain

Summary for 2LVN

• Entry DOI: 10.2210/pdb2lvn/pdb
• Related: 2LVO 2LVP 2LVQ
• NMR Information: BMRB: 18581
• Descriptor: E3 ubiquitin-protein ligase AMFR (1 entity in total)
• Functional Keywords: cue domain, ligase
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein: Q9UKV5
• Total number of polymer chains: 1
• Total formula weight: 5966.75

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: 2024-05-01)

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

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: 23123110
DOI: 10.1016/j.str.2012.09.020

Experimental method

SOLUTION NMR