3L1X

Crystal Structure of U-box Domain of Human E4B Ubiquitin Ligase

3L1X の概要

• エントリーDOI: 10.2210/pdb3l1x/pdb
• 関連するPDBエントリー: 3L1Y 3L1Z
• 分子名称: Ubiquitin conjugation factor E4 B (2 entities in total)
• 機能のキーワード: e3 ubiquitin ligase, e4 ubiquitin ligase, u-box domain, ubl conjugation pathway, ligase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): O95155
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11548.99

構造登録者

Benirschke, R.,Thompson, J.R.,Mer, G. (登録日: 2009-12-14, 公開日: 2010-05-05, 最終更新日: 2023-09-06)

主引用文献

Benirschke, R.C.,Thompson, J.R.,Nomine, Y.,Wasielewski, E.,Juranic, N.,Macura, S.,Hatakeyama, S.,Nakayama, K.I.,Botuyan, M.V.,Mer, G.
Molecular Basis for the Association of Human E4B U Box Ubiquitin Ligase with E2-Conjugating Enzymes UbcH5c and Ubc4.
Structure, 18:955-965, 2010

PubMed Abstract: Human E4B, also called UFD2a, is a U box-containing protein that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor. E4B is thought to participate in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. The U box domain is an anchor site for E2 ubiquitin-conjugating enzymes, but little is known of the binding mechanism. Using X-ray crystallography and NMR spectroscopy, we determined the structures of E4B U box free and bound to UbcH5c and Ubc4 E2s. Whereas previously characterized U box domains are homodimeric, we show that E4B U box is a monomer stabilized by a network of hydrogen bonds identified from scalar coupling measurements. These structural studies, complemented by calorimetry- and NMR-based binding assays, suggest an allosteric regulation of UbcH5c and Ubc4 by E4B U box and provide a molecular basis to understand how the ubiquitylation machinery involving E4B assembles.

PubMed: 20696396
DOI: 10.1016/j.str.2010.04.017

実験手法

X-RAY DIFFRACTION (2.6 Å)