6V9I
cryo-EM structure of Cullin5 bound to RING-box protein 2 (Cul5-Rbx2)
Summary for 6V9I
| Entry DOI | 10.2210/pdb6v9i/pdb |
| EMDB information | 21120 21121 |
| Descriptor | Immunoglobulin G-binding protein G,Cullin-5, RING-box protein 2, ZINC ION (3 entities in total) |
| Functional Keywords | e3 ubiquitin ligase, ring-box protein, ligase |
| Biological source | Streptococcus sp. group G More |
| Total number of polymer chains | 2 |
| Total formula weight | 113374.23 |
| Authors | Komives, E.A.,Lumpkin, R.J.,Baker, R.W.,Leschziner, A.E. (deposition date: 2019-12-13, release date: 2020-04-29, Last modification date: 2024-10-16) |
| Primary citation | Lumpkin, R.J.,Baker, R.W.,Leschziner, A.E.,Komives, E.A. Structure and dynamics of the ASB9 CUL-RING E3 Ligase. Nat Commun, 11:2866-2866, 2020 Cited by PubMed 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. PubMed: 32513959DOI: 10.1038/s41467-020-16499-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.2 Å) |
Structure validation
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