6JM4

The crystal structure of PB1 homo-dimer of human P62/SQSTM1

6JM4 の概要

• エントリーDOI: 10.2210/pdb6jm4/pdb
• 分子名称: Sequestosome-1 (2 entities in total)
• 機能のキーワード: pb1, p62/sqstm1, autophagy, pb1 dimer, signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 45227.22

構造登録者

Shin, H.C.,Lim, D.,Kim, S.J. (登録日: 2019-03-07, 公開日: 2020-01-15, 最終更新日: 2023-11-22)

主引用文献

Lim, D.,Lee, H.S.,Ku, B.,Shin, H.C.,Kim, S.J.
Oligomer Model of PB1 Domain of p62/SQSTM1 Based on Crystal Structure of Homo-Dimer and Calculation of Helical Characteristics.
Mol.Cells, 42:729-738, 2019

PubMed Abstract: Autophagy is an important process for protein recycling. Oligomerization of p62/SQSTM1 is an essential step in this process and is achieved in two steps. Phox and Bem1p (PB1) domains can oligomerize through both basic and acidic surfaces in each molecule. The ZZ-type zinc finger (ZZ) domain binds to target proteins and promotes higheroligomerization of p62. This mechanism is an important step in routing target proteins to the autophagosome. Here, we determined the crystal structure of the PB1 homo-dimer and modeled the p62 PB1 oligomers. These oligomer models were represented by a cylindrical helix and were compared with the previously determined electron microscopic map of a PB1 oligomer. To accurately compare, we mathematically calculated the lead length and radius of the helical oligomers. Our PB1 oligomer model fits the electron microscopy map and is both bendable and stretchable as a flexible helical filament.

PubMed: 31600867
DOI: 10.14348/molcells.2019.0096

実験手法

X-RAY DIFFRACTION (3.20014839602 Å)