التفاصيل البيبلوغرافية
| العنوان: |
C-terminal acidic domain of ubiquitin-conjugating enzymes: A multi-functional conserved intrinsically disordered domain in family 3 of E2 enzymes |
| المؤلفون: |
Luca De Gioia, Elena Papaleo, Alberto Arrigoni, Barbara Grillo, Alessandro Vitriolo |
| المساهمون: |
Arrigoni, A, Grillo, B, Vitriolo, A, DE GIOIA, L, Papaleo, E |
| المصدر: |
Journal of Structural Biology. 178:245-259 |
| بيانات النشر: |
Elsevier BV, 2012. |
| سنة النشر: |
2012 |
| مصطلحات موضوعية: |
E2 enzyme, Molecular Sequence Data, Context (language use), Plasma protein binding, Ubiquitin-conjugating enzyme, Biology, Protein Structure, Secondary, Ubiquitin binding domain, Ubiquitin-Conjugating Enzyme, Protein structure, Ubiquitin, Structural Biology, Humans, Amino Acid Sequence, Structural motif, Intrinsically disorder, Processivity, Protein Structure, Tertiary, Acidic domain, Ubiquitin conjugating enzyme, Biochemistry, Structural biology, Ubiquitin-Conjugating Enzymes, Cdc34, Biophysics, biology.protein, Acidic tail, Human, Protein Binding |
| الوصف: |
E2 ubiquitin-conjugating enzymes are key elements of the ubiquitin (Ub) pathway, since they influence processivity and topology of the Ub chain assembly and, as a consequence, the fate of the target substrates. E2s are multi-domain proteins, with accessory N-terminal or C-terminal domains that can contribute to the specificity for the cognate Ub-like molecules, or even the E3. In this context, the thorough structural characterization of E2 accessory domains is mandatory, in particular when they are associated to specific functions. We here provide, by computational and comparative studies, the first evidence of an acidic domain (AD) conserved in the E2 sub-family 3R. It is an intrinsically disordered domain, in which elements for Ub or E3 recognition are maintained. This conserved acidic domain (AD) shows propensity for α-helix structures (185-192 and 204-218) in the proximity of the sites for interaction with the Ub or the cognate E3. Moreover, our results also suggest that AD can explore conformations with tertiary contacts mainly driven by aromatic and hydrophobic interactions, in absence of its interaction partners. The globular states are likely to be regulated by multiple phosphorylation events, which can trigger conformational changes toward more extended conformations, as judged by MD simulations of the phospho-variants. The extended conformations, in turn, promote the accessibility of the interaction sites for Ub and the E3. We also trace a parallel between this new and natively unfolded structural motif for Ub-recognition and the natively folded ubiquitin associated domain (UBA) typical of family 1 of E2 enzymes, which includes Ubc1. In fact, according to our calculations, Ubc1 maps at the interface between the space of the natively unfolded and folded proteins, as well as it shares common features with the acidic domain of family 3 members. © 2012 Elsevier Inc. |
| تدمد: |
1047-8477 |
| DOI: |
10.1016/j.jsb.2012.04.003 |
| URL الوصول: |
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ffb5ce68d72cc3598038cee1f8a82bb
https://doi.org/10.1016/j.jsb.2012.04.003 |
| Rights: |
CLOSED |
| رقم الانضمام: |
edsair.doi.dedup.....1ffb5ce68d72cc3598038cee1f8a82bb |
| قاعدة البيانات: |
OpenAIRE |