5N9V

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

Summary for 5N9V

Entry DOI	10.2210/pdb5n9v/pdb
NMR Information	BMRB: 34106
Descriptor	NAD(P)(+)--arginine ADP-ribosyltransferase (1 entity in total)
Functional Keywords	beta-grasp, uld, polyubiquitin, transferase
Biological source	Tetrahymena thermophila
Total number of polymer chains	1
Total formula weight	9457.85
Authors	Chiarini, V.,Tossavainen, H. (deposition date: 2017-02-27, release date: 2018-03-21, Last modification date: 2024-06-19)
Primary citation	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 Cited by 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 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation