4ZPZ

Crystal Structure of Semi-synthetic Ubiquitin with Phospho-Ser65 and Ala46Cys

4ZPZ の概要

• エントリーDOI: 10.2210/pdb4zpz/pdb
• 分子名称: Polyubiquitin-B (2 entities in total)
• 機能のキーワード: chromosomal protein, cell signalling, signaling protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Ubiquitin: Cytoplasm : P0CG47
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17377.75

構造登録者

Han, C.,Virdee, S. (登録日: 2015-05-08, 公開日: 2015-06-10, 最終更新日: 2024-11-13)

主引用文献

Han, C.,Pao, K.C.,Kazlauskaite, A.,Muqit, M.M.,Virdee, S.
A Versatile Strategy for the Semisynthetic Production of Ser65 Phosphorylated Ubiquitin and Its Biochemical and Structural Characterisation.
Chembiochem, 16:1574-1579, 2015

PubMed Abstract: Ubiquitin phosphorylation is emerging as an important regulatory layer in the ubiquitin system. This is exemplified by the phosphorylation of ubiquitin on Ser65 by the Parkinson's disease-associated kinase PINK1, which mediates the activation of the E3 ligase Parkin. Additional phosphorylation sites on ubiquitin might also have important cellular roles. Here we report a versatile strategy for preparing phosphorylated ubiquitin. We biochemically and structurally characterise semisynthetic phospho-Ser65-ubiquitin. Unexpectedly, we observed disulfide bond formation between ubiquitin molecules, and hence a novel crystal form. The method outlined provides a direct approach to study the combinatorial effects of phosphorylation on ubiquitin function. Our analysis also suggests that disulfide engineering of ubiquitin could be a useful strategy for obtaining alternative crystal forms of ubiquitin species thereby facilitating structural validation.

PubMed: 26010437
DOI: 10.1002/cbic.201500185

実験手法

X-RAY DIFFRACTION (1.54 Å)