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1O06

Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)

1O06 の概要
エントリーDOI10.2210/pdb1o06/pdb
分子名称Vacuolar protein sorting-associated protein VPS27, ZINC ION (3 entities in total)
機能のキーワードalpha-helix, coiled-coil, tetramer, transport protein
細胞内の位置Endosome membrane; Peripheral membrane protein; Cytoplasmic side: P40343
タンパク質・核酸の鎖数1
化学式量合計2441.58
構造登録者
Fisher, R.D.,Wang, B.,Alam, S.L.,Higginson, D.S.,Rich, R.,Myszka, D.,Sundquist, W.I.,Hill, C.P. (登録日: 2003-02-20, 公開日: 2003-07-22, 最終更新日: 2024-02-14)
主引用文献Fisher, R.D.,Wang, B.,Alam, S.L.,Higginson, D.S.,Robinson, H.,Sundquist, W.I.,Hill, C.P.
Structure and ubiquitin binding of the ubiquitin-interacting motif.
J.Biol.Chem., 278:28976-28984, 2003
Cited by
PubMed Abstract: Ubiquitylation is used to target proteins into a large number of different biological processes including proteasomal degradation, endocytosis, virus budding, and vacuolar protein sorting (Vps). Ubiquitylated proteins are typically recognized using one of several different conserved ubiquitin binding modules. Here, we report the crystal structure and ubiquitin binding properties of one such module, the ubiquitin-interacting motif (UIM). We found that UIM peptides from several proteins involved in endocytosis and vacuolar protein sorting including Hrs, Vps27p, Stam1, and Eps15 bound specifically, but with modest affinity (Kd = 0.1-1 mm), to free ubiquitin. Full affinity ubiquitin binding required the presence of conserved acidic patches at the N and C terminus of the UIM, as well as highly conserved central alanine and serine residues. NMR chemical shift perturbation mapping experiments demonstrated that all of these UIM peptides bind to the I44 surface of ubiquitin. The 1.45 A resolution crystal structure of the second yeast Vps27p UIM (Vps27p-2) revealed that the ubiquitin-interacting motif forms an amphipathic helix. Although Vps27p-2 is monomeric in solution, the motif unexpectedly crystallized as an antiparallel four-helix bundle, and the potential biological implications of UIM oligomerization are therefore discussed.
PubMed: 12750381
DOI: 10.1074/jbc.M302596200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.45 Å)
構造検証レポート
Validation report summary of 1o06
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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