2NBU

Solution structure of the Rad23 ubiquitin-like (UBL) domain

2NBU の概要

• エントリーDOI: 10.2210/pdb2nbu/pdb
• 関連するPDBエントリー: 2NBV 2NBW
• 分子名称: UV excision repair protein RAD23 (1 entity in total)
• 機能のキーワード: dna binding protein
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast)
• 細胞内の位置: Nucleus : P32628
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11039.58

構造登録者

Chen, X.,Walters, K.J. (登録日: 2016-03-12, 公開日: 2016-07-20, 最終更新日: 2024-05-15)

主引用文献

Chen, X.,Randles, L.,Shi, K.,Tarasov, S.G.,Aihara, H.,Walters, K.J.
Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome.
Structure, 24:1257-1270, 2016

PubMed Abstract: Three receptors (Rpn1/S2/PSMD2, Rpn10/S5a, Rpn13/Adrm1) in the proteasome bind substrates by interacting with conjugated ubiquitin chains and/or shuttle factors (Rad23/HR23, Dsk2/PLIC/ubiquilin, Ddi1) that carry ubiquitinated substrates to proteasomes. We solved the structure of two such receptors with their preferred shuttle factor, namely hRpn13(Pru):hPLIC2(UBL) and scRpn1 T1:scRad23(UBL). We find that ubiquitin folds in Rad23 and Dsk2 are fine-tuned by residue substitutions to achieve high affinity for Rpn1 and Rpn13, respectively. A single substitution in hPLIC2 yields enhanced interactions with the Rpn13 ubiquitin contact surface and sterically blocks hRpn13 binding to its preferred ubiquitin chain type, K48-linked chains. Rpn1 T1 binds two ubiquitins in tandem and we find that Rad23 binds exclusively to the higher-affinity Helix28/Helix30 site. Rad23 contacts at Helix28/Helix30 are optimized compared to ubiquitin by multiple conservative amino acid substitutions. Thus, shuttle factors deliver substrates to proteasomes through fine-tuned ubiquitin-like surfaces.

PubMed: 27396824
DOI: 10.1016/j.str.2016.05.018

実験手法

SOLUTION NMR