3OLM

Structure and Function of a Ubiquitin Binding Site within the Catalytic Domain of a HECT Ubiquitin Ligase

3OLM の概要

• エントリーDOI: 10.2210/pdb3olm/pdb
• 分子名称: E3 ubiquitin-protein ligase RSP5, Ubiquitin (3 entities in total)
• 機能のキーワード: ubiquitin e3 ligase, ligase
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Cytoplasm: P39940; Cytoplasm (By similarity): P0CG63
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59207.69

構造登録者

Kim, H.C.,Steffen, A.,Chen, J.,Huibregtse, J.M. (登録日: 2010-08-26, 公開日: 2011-03-23, 最終更新日: 2023-09-06)

主引用文献

Kim, H.C.,Steffen, A.M.,Oldham, M.L.,Chen, J.,Huibregtse, J.M.
Structure and function of a HECT domain ubiquitin-binding site.
Embo Rep., 12:334-341, 2011

PubMed Abstract: The Rsp5 ubiquitin ligase contains a non-covalent binding site for ubiquitin within the amino-terminal lobe (N-lobe) of the HECT domain, and the X-ray crystal structure of the HECT-ubiquitin complex has been determined. Hydrophobic patch residues of ubiquitin (L8, I44, V70) were crucial for interaction with Rsp5, and amino-acid alterations at the Rsp5-binding interface resulted in defects in polyubiquitination. Our results support a model in which the N-lobe-binding site acts to localize and orient the distal end of the ubiquitin chain to promote conjugation of the next ubiquitin molecule.

PubMed: 21399621
DOI: 10.1038/embor.2011.23

実験手法

X-RAY DIFFRACTION (2.495 Å)