6Y75

BIL2 domain from T.thermophila BUBL1 locus (C1A-N143A)

Summary for 6Y75

• Entry DOI: 10.2210/pdb6y75/pdb
• Descriptor: NAD(P)(+)--arginine ADP-ribosyltransferase, DI(HYDROXYETHYL)ETHER, ZINC ION, ... (6 entities in total)
• Functional Keywords: intein, ptm, ubiquitin, splicing
• Biological source: Tetrahymena thermophila (strain SB210); More
• Total number of polymer chains: 4
• Total formula weight: 69978.34

Authors

Ilari, A.,Chiarini, V. (deposition date: 2020-02-28, release date: 2021-02-03, Last modification date: 2024-11-20)

Primary citation

Chiarini, V.,Fiorillo, A.,Camerini, S.,Crescenzi, M.,Nakamura, S.,Battista, T.,Guidoni, L.,Colotti, G.,Ilari, A.
Structural basis of ubiquitination mediated by protein splicing in early Eukarya.
Biochim Biophys Acta Gen Subj, 1865:129844-129844, 2021

PubMed Abstract: Inteins are intervening proteins, which are known to perform protein splicing. The reaction results in the production of an intein domain and an inteinless protein, which shows no trace of the insertion. BIL2 is part of the polyubiquitin locus of Tetrahymena thermophila (BUBL), where two bacterial-intein-like (BIL) domains lacking the C + 1 nucleophile, are flanked by two independent ubiquitin-like domains (ubl4/ubl5).

PubMed: 33444728
DOI: 10.1016/j.bbagen.2021.129844

Experimental method

X-RAY DIFFRACTION (2.3 Å)