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2MWS

Structure of the complex of ubiquitin and the ubiquitin-like (UBL) domain of Ddi1

2MWS の概要
エントリーDOI10.2210/pdb2mws/pdb
NMR情報BMRB: 25088
分子名称Ubiquitin, DNA damage-inducible protein 1 (2 entities in total)
機能のキーワードubl, ddi1, ubiquitin, proteasome, protein transport
由来する生物種Homo sapiens (Human)
詳細
細胞内の位置Ubiquitin: Cytoplasm : P0CG48
Cytoplasm : P40087
タンパク質・核酸の鎖数2
化学式量合計19354.06
構造登録者
Fushman, D.,Nowicka, U.,Walker, O. (登録日: 2014-11-23, 公開日: 2015-03-25, 最終更新日: 2023-06-14)
主引用文献Nowicka, U.,Zhang, D.,Walker, O.,Krutauz, D.,Castaneda, C.A.,Chaturvedi, A.,Chen, T.Y.,Reis, N.,Glickman, M.H.,Fushman, D.
DNA-Damage-Inducible 1 Protein (Ddi1) Contains an Uncharacteristic Ubiquitin-like Domain that Binds Ubiquitin.
Structure, 23:542-557, 2015
Cited by
PubMed Abstract: Ddi1 belongs to a family of shuttle proteins targeting polyubiquitinated substrates for proteasomal degradation. Unlike the other proteasomal shuttles, Rad23 and Dsk2, Ddi1 remains an enigma: its function is not fully understood and structural properties are poorly characterized. We determined the structure and binding properties of the ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains of Ddi1 from Saccharomyces cerevisiae. We found that while Ddi1UBA forms a characteristic UBA:ubiquitin complex, Ddi1UBL has entirely uncharacteristic binding preferences. Despite having a ubiquitin-like fold, Ddi1UBL does not interact with typical UBL receptors but unexpectedly binds ubiquitin, forming a unique interface mediated by hydrophobic contacts and by salt bridges between oppositely charged residues of Ddi1UBL and ubiquitin. In stark contrast to ubiquitin and other UBLs, the β-sheet surface of Ddi1UBL is negatively charged and therefore is recognized in a completely different way. The dual functionality of Ddi1UBL, capable of binding both ubiquitin and proteasome, suggests an intriguing mechanism for Ddi1 as a proteasomal shuttle.
PubMed: 25703377
DOI: 10.1016/j.str.2015.01.010
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2mws
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2026-02-04に公開中

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