Mechanism of ubiquitin recognition by the CUE domain of Vps9p

被引:194
作者
Prag, G
Misra, S
Jones, EA
Ghirlando, R
Davies, BA
Horazdovsky, BF
Hurley, JH [1 ]
机构
[1] NIDDKD, Mol Biol Lab, NIH, Dept Hlth & Human Serv, Bethesda, MD 20892 USA
[2] Mayo Clin & Mayo Fdn, Mayo Clin Canc Ctr, Rochester, MN 55905 USA
[3] Mayo Clin & Mayo Fdn, Dept Biochem & Mol Biol, Rochester, MN 55905 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1016/S0092-8674(03)00364-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Coupling of ubiquitin conjugation to ER degradation (CUE) domains are similar to50 amino acid monoubiquitin binding motifs found in proteins of trafficking and ubiquitination pathways. The 2.3 Angstrom structure of the Vps9p-CUE domain is a dimeric domain-swapped variant of the ubiquitin binding UBA domain. The 1.7 Angstrom 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.
引用
收藏
页码:609 / 620
页数:12
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