2WZK
Structure of the Cul5 N-terminal domain at 2.05A resolution.
Summary for 2WZK
| Entry DOI | 10.2210/pdb2wzk/pdb |
| Related | 3ZKJ |
| Descriptor | CULLIN-5, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | ubl conjugation pathway, hiv, phosphoprotein, isopeptide bond, protein binding |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) |
| Total number of polymer chains | 1 |
| Total formula weight | 45836.32 |
| Authors | Muniz, J.R.C.,Ayinampudi, V.,Zhang, Y.,Babon, J.J.,Chaikuad, A.,Krojer, T.,Pike, A.C.W.,Vollmar, M.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.M.,Weigelt, J.,Bountra, C.,Bullock, A.N. (deposition date: 2009-11-30, release date: 2009-12-15, Last modification date: 2024-05-08) |
| Primary citation | Muniz, J.R.C.,Guo, K.,Kershaw, N.J.,Ayinampudi, V.,von Delft, F.,Babon, J.J.,Bullock, A.N. Molecular Architecture of the Ankyrin Socs Box Family of Cul5-Dependent E3 Ubiquitin Ligases J.Mol.Biol., 425:3166-, 2013 Cited by PubMed Abstract: Multi-subunit Cullin-RING E3 ligases often use repeat domain proteins as substrate-specific adaptors. Structures of these macromolecular assemblies are determined for the F-box-containing leucine-rich repeat and WD40 repeat families, but not for the suppressor of cytokine signaling (SOCS)-box-containing ankyrin repeat proteins (ASB1-18), which assemble with Elongins B and C and Cul5. We determined the crystal structures of the ternary complex of ASB9-Elongin B/C as well as the interacting N-terminal domain of Cul5 and used structural comparisons to establish a model for the complete Cul5-based E3 ligase. The structures reveal a distinct architecture of the ASB9 complex that positions the ankyrin domain coaxial to the SOCS box-Elongin B/C complex and perpendicular to other repeat protein complexes. This alternative architecture appears favorable to present the ankyrin domain substrate-binding site to the E2-ubiquitin, while also providing spacing suitable for bulky ASB9 substrates, such as the creatine kinases. The presented Cul5 structure also differs from previous models and deviates from other Cullins via a rigid-body rotation between Cullin repeats. This work highlights the adaptability of repeat domain proteins as scaffolds in substrate recognition and lays the foundation for future structure-function studies of this important E3 family. PubMed: 23806657DOI: 10.1016/J.JMB.2013.06.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
Download full validation report
