9QUF
Structure of a fungal Ube2O
Summary for 9QUF
| Entry DOI | 10.2210/pdb9quf/pdb |
| Descriptor | Ubiquitin-conjugating enzyme (1 entity in total) |
| Functional Keywords | e2/e3 enzyme, ligase |
| Biological source | Pyrenophora tritici-repentis More |
| Total number of polymer chains | 1 |
| Total formula weight | 97721.21 |
| Authors | Kordic, D.,Williams, T.L.,Luiza Deszcz, L.,Ehrmann, J.,Arnese, R.,Meinhart, A.,Clausen, T. (deposition date: 2025-04-10, release date: 2026-01-21) |
| Primary citation | Kordic, D.,Williams, T.L.,Deszcz, L.,Ehrmann, J.F.,Arnese, R.,Schleiffer, A.,Clausen, T.,Meinhart, A. Structural basis for substrate recruitment and catalytic ubiquitin transfer by the E2/E3 hybrid enzyme UBE2O. J.Biol.Chem., 302:111073-111073, 2025 Cited by PubMed Abstract: UBE2O is a promiscuous ubiquitin ligase involved in cellular quality control pathways. Along with BIRC6, UBE2O is one of only two E2 enzymes that can ubiquitinate substrates in an E3-independent manner. The E2/E3 hybrid targets and multi-monoubiquitinates a multitude of orphan proteins; however, the mechanisms underlying substrate specificity and ubiquitin transfer remain poorly understood. By combining structural and biochemical approaches, we show that substrate binding by UBE2O occurs through a conserved acidic pocket formed by the N-terminal SH3-like domains and that this platform allows the recruitment of a broad range of proteins. Furthermore, we identified specific residues in the catalytic UBC domain that position ubiquitin in a closed state, confirming its confirmation, and priming it for nucleophilic attack by the incoming substrate. Importantly, the activated E2∼Ub conjugate is protected by a tryptophan residue, avoiding premature hydrolysis. By incorporating these findings into the UBC domain of BIRC6 our data provide the molecular basis of how specialized E2/E3 hybrid proteins function as potent ubiquitination enzymes reminiscent of the catalytic principle of RING E3 ligases. PubMed: 41419192DOI: 10.1016/j.jbc.2025.111073 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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