5VZW

TRIM23 RING domain in complex with UbcH5-Ub

5VZW の概要

• エントリーDOI: 10.2210/pdb5vzw/pdb
• 分子名称: Ubiquitin-conjugating enzyme E2 D2, Ubiquitin, E3 ubiquitin-protein ligase TRIM23, ... (5 entities in total)
• 機能のキーワード: ring domain, e3 ligase, transferase-protein binding complex, transferase/protein binding
• 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: 77894.72

構造登録者

Pornillos, O.,Dawidziak, D. (登録日: 2017-05-29, 公開日: 2017-08-09, 最終更新日: 2023-10-04)

主引用文献

Dawidziak, D.M.,Sanchez, J.G.,Wagner, J.M.,Ganser-Pornillos, B.K.,Pornillos, O.
Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase.
Proteins, 85:1957-1961, 2017

PubMed Abstract: Tripartite motif (TRIM) proteins comprise a large family of RING-type ubiquitin E3 ligases that regulate important biological processes. An emerging general model is that TRIMs form elongated antiparallel coiled-coil dimers that prevent interaction of the two attendant RING domains. The RING domains themselves bind E2 conjugating enzymes as dimers, implying that an active TRIM ligase requires higher-order oligomerization of the basal coiled-coil dimers. Here, we report crystal structures of the TRIM23 RING domain in isolation and in complex with an E2-ubiquitin conjugate. Our results indicate that TRIM23 enzymatic activity requires RING dimerization, consistent with the general model of TRIM activation.

PubMed: 28681414
DOI: 10.1002/prot.25348

実験手法

X-RAY DIFFRACTION (2.278 Å)