5N9V

NMR solution structure of ubl5 domain from polyubiquitin locus of T.thermophila.

5N9V の概要

• エントリーDOI: 10.2210/pdb5n9v/pdb
• NMR情報: BMRB: 34106
• 分子名称: NAD(P)(+)--arginine ADP-ribosyltransferase (1 entity in total)
• 機能のキーワード: beta-grasp, uld, polyubiquitin, transferase
• 由来する生物種: Tetrahymena thermophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9457.85

構造登録者

Chiarini, V.,Tossavainen, H. (登録日: 2017-02-27, 公開日: 2018-03-21, 最終更新日: 2024-06-19)

主引用文献

Chiarini, V.,Tossavainen, H.,Sharma, V.,Colotti, G.
NMR structure of a non-conjugatable, ADP-ribosylation associated, ubiquitin-like domain from Tetrahymena thermophila polyubiquitin locus.
Biochim Biophys Acta Gen Subj, 1863:749-759, 2019

PubMed Abstract: Ubiquitin-like domains (UbLs), in addition to being post-translationally conjugated to the target through the E1-E2-E3 enzymatic cascade, can be translated as a part of the protein they ought to regulate. As integral UbLs coexist with the rest of the protein, their structural properties can differ from canonical ubiquitin, depending on the protein context and how they interact with it. In this work, we investigate T.th-ubl5, a UbL present in a polyubiquitin locus of Tetrahymena thermophila, which is integral to an ADP-ribosyl transferase protein. Only one other co-occurrence of these two domains within the same protein has been reported.

PubMed: 30690122
DOI: 10.1016/j.bbagen.2019.01.014

実験手法

SOLUTION NMR