6V9I

cryo-EM structure of Cullin5 bound to RING-box protein 2 (Cul5-Rbx2)

6V9I の概要

• エントリーDOI: 10.2210/pdb6v9i/pdb
• EMDBエントリー: 21120 21121
• 分子名称: Immunoglobulin G-binding protein G,Cullin-5, RING-box protein 2, ZINC ION (3 entities in total)
• 機能のキーワード: e3 ubiquitin ligase, ring-box protein, ligase
• 由来する生物種: Streptococcus sp. group G; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 113374.23

構造登録者

Komives, E.A.,Lumpkin, R.J.,Baker, R.W.,Leschziner, A.E. (登録日: 2019-12-13, 公開日: 2020-04-29, 最終更新日: 2024-10-16)

主引用文献

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

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: 32513959
DOI: 10.1038/s41467-020-16499-9

実験手法

ELECTRON MICROSCOPY (5.2 Å)