1OTR

Solution Structure of a CUE-Ubiquitin Complex

Summary for 1OTR

• Entry DOI: 10.2210/pdb1otr/pdb
• Descriptor: protein Cue2, Ubiquitin (2 entities in total)
• Functional Keywords: protein-protein complex, cell cycle
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 14142.06

Authors

Kang, R.S.,Daniels, C.M.,Salerno, W.J.,Radhakrishnan, I. (deposition date: 2003-03-22, release date: 2003-06-24, Last modification date: 2024-05-22)

Primary citation

Kang, R.S.,Daniels, C.M.,Francis, S.A.,Shih, S.C.,Salerno, W.J.,Hicke, L.,Radhakrishnan, I.
Solution Structure of a CUE-Ubiquitin Complex Reveals a Conserved Mode of Ubiquitin Binding
Cell(Cambridge,Mass.), 113:621-630, 2003

PubMed Abstract: Monoubiquitination serves as a regulatory signal in a variety of cellular processes. Monoubiquitin signals are transmitted by binding to a small but rapidly expanding class of ubiquitin binding motifs. Several of these motifs, including the CUE domain, also promote intramolecular monoubiquitination. The solution structure of a CUE domain of the yeast Cue2 protein in complex with ubiquitin reveals intermolecular interactions involving conserved hydrophobic surfaces, including the Leu8-Ile44-Val70 patch on ubiquitin. The contact surface extends beyond this patch and encompasses Lys48, a site of polyubiquitin chain formation. This suggests an occlusion mechanism for inhibiting polyubiquitin chain formation during monoubiquitin signaling. The CUE domain shares a similar overall architecture with the UBA domain, which also contains a conserved hydrophobic patch. Comparative modeling suggests that the UBA domain interacts analogously with ubiquitin. The structure of the CUE-ubiquitin complex may thus serve as a paradigm for ubiquitin recognition and signaling by ubiquitin binding proteins.

PubMed: 12787503
DOI: 10.1016/S0092-8674(03)00362-3

Experimental method

SOLUTION NMR