7DG2
Nse1-Nse3-Nse4 complex
Summary for 7DG2
| Entry DOI | 10.2210/pdb7dg2/pdb |
| Descriptor | Non-structural maintenance of chromosomes element 1 homolog, MAGE domain-containing protein, Non-structural maintenance of chromosomes element 4, ... (7 entities in total) |
| Functional Keywords | smc, dna binding protein |
| Biological source | Xenopus laevis (African clawed frog) More |
| Total number of polymer chains | 3 |
| Total formula weight | 63280.88 |
| Authors | |
| Primary citation | Jo, A.,Li, S.,Shin, J.W.,Zhao, X.,Cho, Y. Structure Basis for Shaping the Nse4 Protein by the Nse1 and Nse3 Dimer within the Smc5/6 Complex. J.Mol.Biol., 433:166910-166910, 2021 Cited by PubMed Abstract: The Smc5/6 complex facilitates chromosome replication and DNA break repair. Within this complex, a subcomplex composed of Nse1, Nse3 and Nse4 is thought to play multiple roles through DNA binding and regulating ATP-dependent activities of the complex. However, how the Nse1-Nse3-Nse4 subcomplex carries out these multiple functions remain unclear. To address this question, we determine the crystal structure of the Xenopus laevis Nse1-Nse3-Nse4 subcomplex at 1.7 Å resolution and examine how it interacts with DNA. Our structural analyses show that the Nse1-Nse3 dimer adopts a closed conformation and forms three interfaces with a segment of Nse4, forcing it into a Z-shaped conformation. The Nse1-Nse3-Nse4 structure provides an explanation for how the lung disease immunodeficiency and chromosome breakage syndrome-causing mutations could dislodge Nse4 from Nse1-Nse3. Our DNA binding and mutational analyses reveal that the N-terminal and the middle region of Nse4 contribute to DNA interaction and cell viability. Integrating our data with previous crosslink mass spectrometry data, we propose potential roles of the Nse1-Nse3-Nse4 complex in binding DNA within the Smc5/6 complex. PubMed: 33676928DOI: 10.1016/j.jmb.2021.166910 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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