4AUQ

Structure of BIRC7-UbcH5b-Ub complex.

4AUQ の概要

• エントリーDOI: 10.2210/pdb4auq/pdb
• 関連するPDBエントリー: 1C3T 1CMX 1D3Z 1F9J 1FXT 1G6J 1GJZ 1NBF 1OGW 1OXN 1OXQ 1OY7 1Q5W 1S1Q 1SIF 1TBE 1TW6 1UBI 1UBQ 1UD7 1UR6 1W4U 1XD3 1XQQ 1YX5 1YX6 1ZGU 2AYO 2BGF 2C4O 2CLW 2DEN 2ESK 2ESO 2ESP 2ESQ 2FUH 2G45 2GBJ 2GBK 2GBM 2GBN 2GBR 2J7Q 2JF5 2W9N 2WDT 4A49 4A4B 4A4C
• 分子名称: UBIQUITIN-CONJUGATING ENZYME E2 D2, BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 7, POLYUBIQUITIN-C, ... (5 entities in total)
• 機能のキーワード: ligase-ligase-signalling protein complex, ligase/ligase/signalling protein
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 65342.73

構造登録者

Dou, H.,Buetow, L.,Sibbet, G.J.,Cameron, K.,Huang, D.T. (登録日: 2012-05-21, 公開日: 2012-08-15, 最終更新日: 2023-12-20)

主引用文献

Dou, H.,Buetow, L.,Sibbet, G.J.,Cameron, K.,Huang, D.T.
Birc7-E2 Ubiquitin Conjugate Structure Reveals the Mechanism of Ubiquitin Transfer by a Ring Dimer.
Nat.Struct.Mol.Biol., 19:876-, 2012

PubMed Abstract: Certain RING ubiquitin ligases (E3s) dimerize to facilitate ubiquitin (Ub) transfer from ubiquitin-conjugating enzyme (E2) to substrate, but structural evidence on how this process promotes Ub transfer is lacking. Here we report the structure of the human dimeric RING domain from BIRC7 in complex with the E2 UbcH5B covalently linked to Ub (UbcH5B∼Ub). The structure reveals extensive noncovalent donor Ub interactions with UbcH5B and both subunits of the RING domain dimer that stabilize the globular body and C-terminal tail of Ub. Mutations that disrupt these noncovalent interactions or RING dimerization reduce UbcH5B∼Ub binding affinity and ubiquitination activity. Moreover, NMR analyses demonstrate that BIRC7 binding to UbcH5B∼Ub induces peak-shift perturbations in the donor Ub consistent with the crystallographically-observed Ub interactions. Our results provide structural insights into how dimeric RING E3s recruit E2∼Ub and optimize the donor Ub configuration for transfer.

PubMed: 22902369
DOI: 10.1038/NSMB.2379

実験手法

X-RAY DIFFRACTION (2.176 Å)