التفاصيل البيبلوغرافية
| العنوان: |
Structure and dynamics of the ASB9 CUL-RING E3 Ligase |
| المؤلفون: |
Ryan J. Lumpkin, Richard W. Baker, Andres E. Leschziner, Elizabeth A. Komives |
| المصدر: |
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020) |
| بيانات النشر: |
Nature Portfolio, 2020. |
| سنة النشر: |
2020 |
| المجموعة: |
LCC:Science |
| مصطلحات موضوعية: |
Science |
| الوصف: |
Abstract The Cullin 5 (CUL5) Ring E3 ligase uses adaptors Elongins B and C (ELOB/C) to bind different SOCS-box-containing substrate receptors, determining the substrate specificity of the ligase. The 18-member ankyrin and SOCS box (ASB) family is the largest substrate receptor family. Here we report cryo-EM data for the substrate, creatine kinase (CKB) bound to ASB9-ELOB/C, and for full-length CUL5 bound to the RING protein, RBX2, which binds various E2s. To date, no full structures are available either for a substrate-bound ASB nor for CUL5. Hydrogen–deuterium exchange (HDX-MS) mapped onto a full structural model of the ligase revealed long-range allostery extending from the substrate through CUL5. We propose a revised allosteric mechanism for how CUL-E3 ligases function. ASB9 and CUL5 behave as rigid rods, connected through a hinge provided by ELOB/C transmitting long-range allosteric crosstalk from the substrate through CUL5 to the RBX2 flexible linker. |
| نوع الوثيقة: |
article |
| وصف الملف: |
electronic resource |
| اللغة: |
English |
| تدمد: |
2041-1723 |
| Relation: |
https://doaj.org/toc/2041-1723 |
| DOI: |
10.1038/s41467-020-16499-9 |
| URL الوصول: |
https://doaj.org/article/0bbb6cb9e2c74688aa91f0f7c786a41f |
| رقم الانضمام: |
edsdoj.0bbb6cb9e2c74688aa91f0f7c786a41f |
| قاعدة البيانات: |
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