6TMM
BIL2 domain from T.thermophila BUBL1 locus (C1A-N143A)
This is a non-PDB format compatible entry.
Summary for 6TMM
| Entry DOI | 10.2210/pdb6tmm/pdb |
| Descriptor | NAD(P)(+)--arginine ADP-ribosyltransferase, FORMIC ACID, DI(HYDROXYETHYL)ETHER, ... (7 entities in total) |
| Functional Keywords | intein, ptm, ubiquitin, splicing |
| Biological source | Tetrahymena thermophila SB210 More |
| Total number of polymer chains | 4 |
| Total formula weight | 72597.56 |
| Authors | Chiarini, V.,Ilari, A. (deposition date: 2019-12-04, release date: 2020-12-16, 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 Cited by 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: 33444728DOI: 10.1016/j.bbagen.2021.129844 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.398 Å) |
Structure validation
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