1mn3
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Cue domain of yeast Vps9p
OverviewOverview
Coupling of ubiquitin conjugation to ER degradation (CUE) domains are, approximately 50 amino acid monoubiquitin binding motifs found in proteins, of trafficking and ubiquitination pathways. The 2.3 A structure of the, Vps9p-CUE domain is a dimeric domain-swapped variant of the ubiquitin, binding UBA domain. The 1.7 A structure of the CUE:ubiquitin complex shows, that one CUE dimer binds one ubiquitin molecule. The bound CUE dimer is, kinked relative to the unbound CUE dimer and wraps around ubiquitin. The, CUE monomer contains two ubiquitin binding surfaces on opposite faces of, the molecule that cannot bind simultaneously to a single ubiquitin, molecule. Dimerization of the CUE domain allows both surfaces to contact a, single ubiquitin molecule, providing a mechanism for high-affinity binding, to monoubiquitin.
About this StructureAbout this Structure
1MN3 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Mechanism of ubiquitin recognition by the CUE domain of Vps9p., Prag G, Misra S, Jones EA, Ghirlando R, Davies BA, Horazdovsky BF, Hurley JH, Cell. 2003 May 30;113(5):609-20. PMID:12787502
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