1MN3

Cue domain of yeast Vps9p

1MN3 の概要

• エントリーDOI: 10.2210/pdb1mn3/pdb
• 分子名称: Vacuolar protein sorting-associated protein VPS9 (2 entities in total)
• 機能のキーワード: ubiquitin, protein transport
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P54787
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6222.83

構造登録者

Prag, G.,Misra, S.,Jones, E.,Ghirlando, R.,Davies, B.A.,Horazdovsky, B.F.,Hurley, J.H. (登録日: 2002-09-04, 公開日: 2003-06-10, 最終更新日: 2024-11-06)

主引用文献

Prag, G.,Misra, S.,Jones, E.A.,Ghirlando, R.,Davies, B.A.,Horazdovsky, B.F.,Hurley, J.H.
Mechanism of Ubiquitin Recognition by the CUE Domain of Vps9p
Cell(Cambridge,Mass.), 113:609-620, 2003

PubMed Abstract: 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.

PubMed: 12787502
DOI: 10.1016/S0092-8674(03)00364-7

実験手法

X-RAY DIFFRACTION (2.3 Å)