6JM4
The crystal structure of PB1 homo-dimer of human P62/SQSTM1
Summary for 6JM4
| Entry DOI | 10.2210/pdb6jm4/pdb |
| Descriptor | Sequestosome-1 (2 entities in total) |
| Functional Keywords | pb1, p62/sqstm1, autophagy, pb1 dimer, signaling protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 45227.22 |
| Authors | Shin, H.C.,Lim, D.,Kim, S.J. (deposition date: 2019-03-07, release date: 2020-01-15, Last modification date: 2023-11-22) |
| Primary citation | 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 Cited by 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: 31600867DOI: 10.14348/molcells.2019.0096 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.20014839602 Å) |
Structure validation
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