2EHO
Crystal structure of human GINS complex
Summary for 2EHO
| Entry DOI | 10.2210/pdb2eho/pdb |
| Descriptor | GINS complex subunit 4, DNA replication complex GINS protein PSF1, DNA replication complex GINS protein PSF2, ... (6 entities in total) |
| Functional Keywords | protein-protein complex, 4-helical bundle, hydrophobic interaction, replication |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm (By similarity): Q9BRT9 Nucleus (By similarity): Q14691 Q9Y248 Q9BRX5 |
| Total number of polymer chains | 12 |
| Total formula weight | 270086.14 |
| Authors | Choi, J.M.,Lim, H.S.,Kim, J.J.,Song, O.K.,Cho, Y. (deposition date: 2007-03-07, release date: 2007-06-19, Last modification date: 2024-10-30) |
| Primary citation | Choi, J.M.,Lim, H.S.,Kim, J.J.,Song, O.K.,Cho, Y. Crystal structure of the human GINS complex Genes Dev., 21:1316-1321, 2007 Cited by PubMed Abstract: The GINS complex mediates the assembly of the MCM2-7 (minichromosome maintenance) complex with proteins in a replisome progression complex. The eukaryotic GINS complex is composed of Sld5, Psf1, Psf2, and Psf3, which must be assembled for cell proliferation. We determined the crystal structure of the human GINS complex: GINS forms an elliptical shape with a small central channel. The structures of Sld5 and Psf2 resemble those of Psf1 and Psf3, respectively. In addition, the N-terminal and C-terminal domains of Sld5/Psf1 are permuted in Psf2/Psf3, which suggests that the four proteins have evolved from a common ancestor. Using a structure-based mutational analysis, we identified the functionally critical surface regions of the GINS complex. PubMed: 17545466DOI: 10.1101/gad.1548107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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